Systemic lupus erythematosus: Molecular cloning of fourteen recombinant DNase monoclonal kappa light chains with different catalytic properties

DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies. An immunoglobulin light chain phagemid library derived from peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) was used. The small pools of phage particles displaying DN...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1840; no. 6; pp. 1725 - 1737
Main Authors Kostrikina, Irina A., Buneva, Valentina N., Nevinsky, Georgy A.
Format Journal Article
LanguageEnglish
Published Netherlands 01.06.2014
Subjects
affinity chromatography
antibodies
Antibody Affinity
bacteriophages
calcium
Catalysis
cations
clones
Cloning, Molecular
cobalt
copper
deoxyribonucleases
Deoxyribonucleases - immunology
divalent metals
DNA
Escherichia coli
gel chromatography
Humans
Hydrogen-Ion Concentration
hydrolysis
Immunoglobulin kappa-Chains - genetics
immunoglobulin light chains
lupus erythematosus
Lupus Erythematosus, Systemic - immunology
lymphocytes
magnesium
Magnesium - pharmacology
manganese
Manganese - pharmacology
molecular cloning
nickel
pathogenesis
patients
potassium chloride
Recombinant Proteins - biosynthesis
sodium chloride
zinc
DNase activity
Systemic lupus erythematosus
Recombinant monoclonal light chain
Extreme diversity
Online AccessGet full text

Cover

Abstract DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies. An immunoglobulin light chain phagemid library derived from peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) was used. The small pools of phage particles displaying DNA binding light chains with different for DNA were isolated by affinity chromatography on DNA-cellulose and the fraction eluted with 0.5M NaCl was used for preparation of individual monoclonal light chains (MLChs, 28kDa). Forty-five of 451 individual colonies were randomly chosen for a study of MLChs with DNase activity. The clones were expressed in Escherichia coli in a soluble form, and MLChs were purified by metal chelating chromatography followed by gel filtration, and studied in detail. Fifteen of 45 MLChs efficiently hydrolyzed DNA, and fourteen of them demonstrated various optimal concentrations of KCl or NaCl in a 1-100mM range and showed one or two pH optima in a 4.8-9.1 range. All MLChs were dependent on divalent metal cations: the ratio of relative DNase activity in the presence of Mn(2+), Ca(2+), Mg(2+), Ni(2+), Zn(2+), Cu(2+), and Co(2+) was individual for each MLCh preparation. Fourteen MLChs demonstrated a comparable affinity for DNA (260-320nM), but different kcat values (0.02-0.7min(-1)). These observations suggest an extreme diversity of DNase abzymes from SLE patients. SLE light chain repertoire can serve as a source of new types of DNases.
AbstractList DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies.BACKGROUNDDNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies.An immunoglobulin light chain phagemid library derived from peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) was used. The small pools of phage particles displaying DNA binding light chains with different for DNA were isolated by affinity chromatography on DNA-cellulose and the fraction eluted with 0.5M NaCl was used for preparation of individual monoclonal light chains (MLChs, 28kDa). Forty-five of 451 individual colonies were randomly chosen for a study of MLChs with DNase activity. The clones were expressed in Escherichia coli in a soluble form, and MLChs were purified by metal chelating chromatography followed by gel filtration, and studied in detail.METHODSAn immunoglobulin light chain phagemid library derived from peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) was used. The small pools of phage particles displaying DNA binding light chains with different for DNA were isolated by affinity chromatography on DNA-cellulose and the fraction eluted with 0.5M NaCl was used for preparation of individual monoclonal light chains (MLChs, 28kDa). Forty-five of 451 individual colonies were randomly chosen for a study of MLChs with DNase activity. The clones were expressed in Escherichia coli in a soluble form, and MLChs were purified by metal chelating chromatography followed by gel filtration, and studied in detail.Fifteen of 45 MLChs efficiently hydrolyzed DNA, and fourteen of them demonstrated various optimal concentrations of KCl or NaCl in a 1-100mM range and showed one or two pH optima in a 4.8-9.1 range. All MLChs were dependent on divalent metal cations: the ratio of relative DNase activity in the presence of Mn(2+), Ca(2+), Mg(2+), Ni(2+), Zn(2+), Cu(2+), and Co(2+) was individual for each MLCh preparation. Fourteen MLChs demonstrated a comparable affinity for DNA (260-320nM), but different kcat values (0.02-0.7min(-1)).RESULTSFifteen of 45 MLChs efficiently hydrolyzed DNA, and fourteen of them demonstrated various optimal concentrations of KCl or NaCl in a 1-100mM range and showed one or two pH optima in a 4.8-9.1 range. All MLChs were dependent on divalent metal cations: the ratio of relative DNase activity in the presence of Mn(2+), Ca(2+), Mg(2+), Ni(2+), Zn(2+), Cu(2+), and Co(2+) was individual for each MLCh preparation. Fourteen MLChs demonstrated a comparable affinity for DNA (260-320nM), but different kcat values (0.02-0.7min(-1)).These observations suggest an extreme diversity of DNase abzymes from SLE patients.CONCLUSIONSThese observations suggest an extreme diversity of DNase abzymes from SLE patients.SLE light chain repertoire can serve as a source of new types of DNases.GENERAL SIGNIFICANCESLE light chain repertoire can serve as a source of new types of DNases.
DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies.An immunoglobulin light chain phagemid library derived from peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) was used. The small pools of phage particles displaying DNA binding light chains with different for DNA were isolated by affinity chromatography on DNA-cellulose and the fraction eluted with 0.5M NaCl was used for preparation of individual monoclonal light chains (MLChs, 28kDa). Forty-five of 451 individual colonies were randomly chosen for a study of MLChs with DNase activity. The clones were expressed in Escherichia coli in a soluble form, and MLChs were purified by metal chelating chromatography followed by gel filtration, and studied in detail.Fifteen of 45 MLChs efficiently hydrolyzed DNA, and fourteen of them demonstrated various optimal concentrations of KCl or NaCl in a 1–100mM range and showed one or two pH optima in a 4.8–9.1 range. All MLChs were dependent on divalent metal cations: the ratio of relative DNase activity in the presence of Mn2+, Ca2+, Mg2+, Ni2+, Zn2+, Cu2+, and Co2+ was individual for each MLCh preparation. Fourteen MLChs demonstrated a comparable affinity for DNA (260–320nM), but different kcat values (0.02–0.7min−1).These observations suggest an extreme diversity of DNase abzymes from SLE patients.SLE light chain repertoire can serve as a source of new types of DNases.
DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies. An immunoglobulin light chain phagemid library derived from peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) was used. The small pools of phage particles displaying DNA binding light chains with different for DNA were isolated by affinity chromatography on DNA-cellulose and the fraction eluted with 0.5M NaCl was used for preparation of individual monoclonal light chains (MLChs, 28kDa). Forty-five of 451 individual colonies were randomly chosen for a study of MLChs with DNase activity. The clones were expressed in Escherichia coli in a soluble form, and MLChs were purified by metal chelating chromatography followed by gel filtration, and studied in detail. Fifteen of 45 MLChs efficiently hydrolyzed DNA, and fourteen of them demonstrated various optimal concentrations of KCl or NaCl in a 1-100mM range and showed one or two pH optima in a 4.8-9.1 range. All MLChs were dependent on divalent metal cations: the ratio of relative DNase activity in the presence of Mn(2+), Ca(2+), Mg(2+), Ni(2+), Zn(2+), Cu(2+), and Co(2+) was individual for each MLCh preparation. Fourteen MLChs demonstrated a comparable affinity for DNA (260-320nM), but different kcat values (0.02-0.7min(-1)). These observations suggest an extreme diversity of DNase abzymes from SLE patients. SLE light chain repertoire can serve as a source of new types of DNases.
Author Buneva, Valentina N.
Nevinsky, Georgy A.
Kostrikina, Irina A.
Author_xml – sequence: 1
  givenname: Irina A.
  surname: Kostrikina
  fullname: Kostrikina, Irina A.
– sequence: 2
  givenname: Valentina N.
  surname: Buneva
  fullname: Buneva, Valentina N.
– sequence: 3
  givenname: Georgy A.
  surname: Nevinsky
  fullname: Nevinsky, Georgy A.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/24462577$$D View this record in MEDLINE/PubMed
BookMark eNqFkTtvFDEUhV0EkQf8A4Rc0uzEr5ndSYfCI0gBCtJb157rXS8ee7A9ivZX8JeZ1SYNBdzmNt85RzrnkpzFFJGQN5w1nPHuet8YA1uMjWBcNYw3TKzPyAWTTK0U79pzclnKni3X9u1Lci6U6kS7Xl-Q3z8OpeLoLQ3zNBeK-VB3OEJNZS439GsKaOcAmdqQoo9bmhx1ac4VMdKMNo3GR4iVfvgGBemYYjqSEOhPmCagwW93ldod-Fjoo687OnjnMOMisVAhHOqSPeU0Ya4eyyvywkEo-PrpX5GHTx8fbu9W998_f7l9f7-yUrG6clYikz0zphssY6Bca0WPMHBrBEq7gXUv16IVvWPojBvQbEAKpoQ01kh5Rd6dbJfkXzOWqkdfLIYAEdNctFiq4n2rWPdflLe838iuZ2xB3z6hsxlx0FP2I-SDfq57AW5OgM2plIxOW1-h-hRrBh80Z_q4p97r0576uKdmXC97LmL1l_jZ_5-yP4Q7rMg
CitedBy_id crossref_primary_10_1016_j_placenta_2018_06_007
crossref_primary_10_1093_intimm_dxv042
crossref_primary_10_1002_bab_1858
crossref_primary_10_1134_S0026893317060036
crossref_primary_10_1371_journal_pone_0183867
crossref_primary_10_3390_ijms23158102
crossref_primary_10_3389_fimmu_2019_01667
crossref_primary_10_1002_jmr_2559
crossref_primary_10_3390_ijms23169182
crossref_primary_10_1002_jmr_2476
crossref_primary_10_1098_rsob_150064
crossref_primary_10_3390_biomedicines10102663
crossref_primary_10_1134_S0006297915020054
crossref_primary_10_3389_fimmu_2021_808008
crossref_primary_10_3389_fimmu_2024_1346619
Cites_doi 10.1016/j.molimm.2006.12.005
10.1016/S0022-1759(02)00233-8
10.1016/0925-4439(96)00028-2
10.1385/ABAB:83:1-3:115
10.1006/jmbi.1997.1196
10.1126/science.2727702
10.1021/bi035038d
10.1016/S0165-2478(02)00006-8
10.4049/jimmunol.155.5.2695
10.1016/0090-1229(89)90030-5
10.1038/nrrheum.2011.153
10.1007/BF02787705
10.1038/352624a0
10.1023/A:1008826909441
10.1016/S0021-9258(18)98440-1
10.1073/pnas.92.1.254
10.1126/science.7569920
10.1111/j.1582-4934.2003.tb00227.x
10.3233/NIB-2012-012042
10.1016/0968-0004(87)90208-8
10.1007/BF02787704
10.1002/jmr.743
10.1159/000058801
10.1007/BF02787709
10.1100/tsw.2010.98
10.1016/S0165-2478(01)00185-7
10.1073/pnas.0509849103
10.1073/pnas.98.4.1793
10.1385/ABAB:83:1-3:85
10.1023/A:1009252200231
10.1126/science.1585181
10.1016/j.bbapap.2007.05.006
10.1007/BF02787708
10.1016/S0168-1656(98)00009-1
10.1002/jmr.300070203
10.1002/bit.20031
10.1111/j.1582-4934.2009.00738.x
10.1007/BF02787932
10.3109/08830189309061698
10.1006/jmbi.1996.0703
10.1007/BF00243760
10.1016/S0962-8924(99)01682-7
10.1016/S0161-5890(97)00129-6
10.1074/jbc.M705674200
10.1002/jmr.890
10.1074/jbc.M102530200
10.1385/ABAB:83:1-3:71
10.1073/pnas.200360497
10.1016/S0021-9258(19)85765-4
10.1002/jmr.1016
10.1073/pnas.90.19.8876
10.1371/journal.pcbi.1001000
10.1016/j.bmcl.2004.06.044
10.1016/S0014-5793(97)01163-0
10.1021/bi992588w
10.1073/pnas.92.6.2145
10.1016/S0022-1759(02)00234-X
10.1016/j.biochi.2010.01.022
10.1111/j.1582-4934.2004.tb00325.x
10.1134/S0026893306050128
10.1016/0165-2478(88)90043-0
10.1093/intimm/dxn061
10.1016/j.imlet.2005.10.018
10.1093/intimm/dxs071
10.1074/jbc.270.25.15257
10.1002/jmr.923
10.1074/jbc.M600937200
10.1007/BF02787937
10.1016/S0165-2478(03)00042-7
10.1002/jmr.906
10.1093/intimm/dxp004
ContentType Journal Article
Copyright Copyright © 2014 Elsevier B.V. All rights reserved.
Copyright_xml – notice: Copyright © 2014 Elsevier B.V. All rights reserved.
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7S9
L.6
DOI 10.1016/j.bbagen.2014.01.027
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList MEDLINE - Academic
AGRICOLA
MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
Biology
EndPage 1737
ExternalDocumentID 24462577
10_1016_j_bbagen_2014_01_027
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
23N
3O-
4.4
457
4G.
53G
5GY
5RE
5VS
7-5
71M
8P~
9JM
AAEDT
AAEDW
AAHBH
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AATTM
AAXKI
AAXUO
AAYWO
AAYXX
ABEFU
ABFNM
ABGSF
ABMAC
ABUDA
ABWVN
ABXDB
ACDAQ
ACIUM
ACRLP
ACRPL
ACVFH
ADBBV
ADCNI
ADEZE
ADMUD
ADNMO
ADUVX
AEBSH
AEHWI
AEIPS
AEKER
AEUPX
AFJKZ
AFPUW
AFTJW
AFXIZ
AGCQF
AGHFR
AGQPQ
AGRDE
AGRNS
AGUBO
AGYEJ
AHHHB
AIEXJ
AIGII
AIIUN
AIKHN
AITUG
AKBMS
AKRWK
AKYEP
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
ANKPU
APXCP
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
BNPGV
CITATION
CS3
EBS
EFJIC
EJD
EO8
EO9
EP2
EP3
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HLW
HVGLF
HZ~
IHE
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OHT
OZT
P-8
P-9
PC.
Q38
R2-
ROL
RPZ
SBG
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SSH
SSU
SSZ
T5K
UQL
WH7
WUQ
XJT
XPP
~G-
-~X
.55
.GJ
AAYJJ
ABJNI
AFFNX
AI.
CGR
CUY
CVF
ECM
EIF
F5P
H~9
K-O
MVM
NPM
RIG
TWZ
UHS
VH1
X7M
Y6R
YYP
ZE2
ZGI
~KM
7X8
7S9
L.6
ID FETCH-LOGICAL-c340t-fc3e0390bb6dc00a4f5c29ead1cb2e3c8a79372529f0efbfdeb8a320423bcb33
ISSN 0304-4165
0006-3002
IngestDate Fri Jul 11 07:01:01 EDT 2025
Fri Jul 11 01:38:56 EDT 2025
Mon Jul 21 05:55:13 EDT 2025
Thu Apr 24 23:01:06 EDT 2025
Tue Jul 01 00:22:03 EDT 2025
IsPeerReviewed true
IsScholarly true
Issue 6
Keywords DNase activity
Systemic lupus erythematosus
Recombinant monoclonal light chain
Extreme diversity
Language English
License Copyright © 2014 Elsevier B.V. All rights reserved.
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c340t-fc3e0390bb6dc00a4f5c29ead1cb2e3c8a79372529f0efbfdeb8a320423bcb33
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 24462577
PQID 1519836900
PQPubID 23479
PageCount 13
ParticipantIDs proquest_miscellaneous_2000195406
proquest_miscellaneous_1519836900
pubmed_primary_24462577
crossref_citationtrail_10_1016_j_bbagen_2014_01_027
crossref_primary_10_1016_j_bbagen_2014_01_027
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2014-06-01
PublicationDateYYYYMMDD 2014-06-01
PublicationDate_xml – month: 06
  year: 2014
  text: 2014-06-01
  day: 01
PublicationDecade 2010
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Biochimica et biophysica acta
PublicationTitleAlternate Biochim Biophys Acta
PublicationYear 2014
References Paul (10.1016/j.bbagen.2014.01.027_bb0150) 1995; 270
McCafferty (10.1016/j.bbagen.2014.01.027_bb0340) 1994; 47
Polosukhina (10.1016/j.bbagen.2014.01.027_bb0160) 2005; 11
Sun (10.1016/j.bbagen.2014.01.027_bb0265) 1997; 271
Andrievskaya (10.1016/j.bbagen.2014.01.027_bb0110) 2000; 6
Hu (10.1016/j.bbagen.2014.01.027_bb0095) 1998; 61
Paul (10.1016/j.bbagen.2014.01.027_bb0330) 2001; 276
Clackson (10.1016/j.bbagen.2014.01.027_bb0335) 1991; 352
Baranovskii (10.1016/j.bbagen.2014.01.027_bb0125) 2001; 76
Kim (10.1016/j.bbagen.2014.01.027_bb0320) 2006; 281
Gueroult (10.1016/j.bbagen.2014.01.027_bb0410) 2010; 6
Thiagarajan (10.1016/j.bbagen.2014.01.027_bb0235) 2000; 77
Krasnorutskii (10.1016/j.bbagen.2014.01.027_bb0350) 2008; 21
Williamson (10.1016/j.bbagen.2014.01.027_bb0445) 2001; 98
Mitsuda (10.1016/j.bbagen.2014.01.027_bb0255) 2004; 86
Nishi (10.1016/j.bbagen.2014.01.027_bb0425) 2002; 269
Avalle (10.1016/j.bbagen.2014.01.027_bb0090) 1998; 75
Izadyar (10.1016/j.bbagen.2014.01.027_bb0100) 1993; 90
Rangan (10.1016/j.bbagen.2014.01.027_bb0270) 2003; 42
Nishiyama (10.1016/j.bbagen.2014.01.027_bb0245) 2007; 44
Polosukhina (10.1016/j.bbagen.2014.01.027_bb0155) 2004; 8
Odintsova (10.1016/j.bbagen.2014.01.027_bb0305) 2006; 40
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0055) 2010; 10
Mitsuhashi (10.1016/j.bbagen.2014.01.027_bb0440) 1978; 20
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0065) 2011
Friboulet (10.1016/j.bbagen.2014.01.027_bb0085) 1994; 47
Kozyr (10.1016/j.bbagen.2014.01.027_bb0295) 1998; 75
(10.1016/j.bbagen.2014.01.027_bb0030) 2005
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0035) 2002; 269
Baranovskii (10.1016/j.bbagen.2014.01.027_bb0120) 1998; 63
Odintsova (10.1016/j.bbagen.2014.01.027_bb0175) 2005; 18
Parkhomenko (10.1016/j.bbagen.2014.01.027_bb0390) 2010; 92
Parkhomenko (10.1016/j.bbagen.2014.01.027_bb0180) 2010; 23
Krasnorutskii (10.1016/j.bbagen.2014.01.027_bb0365) 2009; 21
Kanyshkova (10.1016/j.bbagen.2014.01.027_bb0215) 1997; 416
Kozyr (10.1016/j.bbagen.2014.01.027_bb0325) 2012; 2012
Shoenfeld (10.1016/j.bbagen.2014.01.027_bb0285) 1988; 17
Lerner (10.1016/j.bbagen.2014.01.027_bb0010) 1995; 73
Paul (10.1016/j.bbagen.2014.01.027_bb0070) 1989; 244
Frese (10.1016/j.bbagen.2014.01.027_bb0310) 2011; 7
Mei (10.1016/j.bbagen.2014.01.027_bb0205) 1991; 266
Kalaga (10.1016/j.bbagen.2014.01.027_bb0145) 1995; 155
Bezuglova (10.1016/j.bbagen.2014.01.027_bb0190) 2012; 24
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0220) 2000; 83
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0040) 2002
Martin (10.1016/j.bbagen.2014.01.027_bb0025) 1999; 9
Hifumi (10.1016/j.bbagen.2014.01.027_bb0250) 2008; 283
Jones (10.1016/j.bbagen.2014.01.027_bb0405) 1996; 264
Galvita (10.1016/j.bbagen.2014.01.027_bb0210) 2007; 1
Tawfik (10.1016/j.bbagen.2014.01.027_bb0430) 2002; 92
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0450) 2012; 3
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0050) 2005
Paul (10.1016/j.bbagen.2014.01.027_bb0195) 1998; 75
Thiagarajan (10.1016/j.bbagen.2014.01.027_bb0230) 2000; 39
Stewart (10.1016/j.bbagen.2014.01.027_bb0020) 1993; 10
Andrievskaya (10.1016/j.bbagen.2014.01.027_bb0115) 2002; 81
Shoenfeld (10.1016/j.bbagen.2014.01.027_bb0290) 1989; 51
Buneva (10.1016/j.bbagen.2014.01.027_bb0080) 1994; 28
Krasnorutskii (10.1016/j.bbagen.2014.01.027_bb0360) 2008; 20
Kolesnikov (10.1016/j.bbagen.2014.01.027_bb0105) 2000; 97
Krasnorutskii (10.1016/j.bbagen.2014.01.027_bb0355) 2008; 21
Baranovskii (10.1016/j.bbagen.2014.01.027_bb0300) 1998; 63
Bernardi (10.1016/j.bbagen.2014.01.027_bb0380) 1971
Buneva (10.1016/j.bbagen.2014.01.027_bb0225) 1998; 75
Campbell (10.1016/j.bbagen.2014.01.027_bb0415) 1980; 255
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0045) 2003; 7
Hifumi (10.1016/j.bbagen.2014.01.027_bb0400) 2000; 13
Baranovskii (10.1016/j.bbagen.2014.01.027_bb0385) 2008; 2
Suck (10.1016/j.bbagen.2014.01.027_bb0375) 1994; 7
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0060) 2010
Sinohara (10.1016/j.bbagen.2014.01.027_bb0200) 2000; 83
Paul (10.1016/j.bbagen.2014.01.027_bb0240) 2000; 83
Kubota (10.1016/j.bbagen.2014.01.027_bb0435) 1977; 44
Gololobov (10.1016/j.bbagen.2014.01.027_bb0420) 1995; 92
Fersht (10.1016/j.bbagen.2014.01.027_bb0370) 1985
Pisetsky (10.1016/j.bbagen.2014.01.027_bb0280) 2001; 3
Taguchi (10.1016/j.bbagen.2014.01.027_bb0275) 2004; 14
Schultz (10.1016/j.bbagen.2014.01.027_bb0015) 1995; 269
Kuznetsova (10.1016/j.bbagen.2014.01.027_bb0345) 2007; 1774
Nevinsky (10.1016/j.bbagen.2014.01.027_bb0130) 2001; 7
Polosukhina (10.1016/j.bbagen.2014.01.027_bb0165) 2006; 103
Gololobov (10.1016/j.bbagen.2014.01.027_bb0315) 1997; 34
Tolmacheva (10.1016/j.bbagen.2014.01.027_bb0395) 2009; 22
Ponomarenko (10.1016/j.bbagen.2014.01.027_bb0170) 2006; 103
Legostaeva (10.1016/j.bbagen.2014.01.027_bb0185) 2010; 14
Lerner (10.1016/j.bbagen.2014.01.027_bb0005) 1987; 12
Tyutyulkova (10.1016/j.bbagen.2014.01.027_bb0260) 1996; 1316
Savel'ev (10.1016/j.bbagen.2014.01.027_bb0135) 1999; 6
Savel'ev (10.1016/j.bbagen.2014.01.027_bb0140) 2003; 86
Shuster (10.1016/j.bbagen.2014.01.027_bb0075) 1992; 256
References_xml – start-page: 151
  year: 2011
  ident: 10.1016/j.bbagen.2014.01.027_bb0065
  article-title: Natural catalytic antibodies in norm and in HIV-infected patients
– volume: 44
  start-page: 2707
  year: 2007
  ident: 10.1016/j.bbagen.2014.01.027_bb0245
  article-title: Antibodies to the superantigenic site of HIV-1 gp120: hydrolytic and binding activities of the light chain subunit
  publication-title: Mol. Immunol.
  doi: 10.1016/j.molimm.2006.12.005
– start-page: 505
  year: 2005
  ident: 10.1016/j.bbagen.2014.01.027_bb0050
  article-title: Natural catalytic antibodies — abzymes
– volume: 269
  start-page: 213
  year: 2002
  ident: 10.1016/j.bbagen.2014.01.027_bb0425
  article-title: Evolution of catalytic antibody repertoire in autoimmune mice
  publication-title: J. Immunol. Methods
  doi: 10.1016/S0022-1759(02)00233-8
– volume: 1316
  start-page: 217
  year: 1996
  ident: 10.1016/j.bbagen.2014.01.027_bb0260
  article-title: Efficient vasoactive intestinal polypeptide hydrolyzing autoantibody light chains selected by phage display
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0925-4439(96)00028-2
– volume: 7
  start-page: 201
  year: 2001
  ident: 10.1016/j.bbagen.2014.01.027_bb0130
  article-title: Effect of different drugs on the level of DNA-hydrolyzing polyclonal IgG antibodies in sera of patients with Hashimoto's thyroiditis and nontoxic nodal goiter
  publication-title: Med. Sci. Monit.
– volume: 83
  start-page: 115
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0220
  article-title: Secretory immunoglobulin A from healthy human mothers' milk catalyzes nucleic acid hydrolysis
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1385/ABAB:83:1-3:115
– start-page: 1
  year: 2002
  ident: 10.1016/j.bbagen.2014.01.027_bb0040
  article-title: Natural catalytic antibodies — new characters in the protein repertoire
– volume: 271
  start-page: 374
  year: 1997
  ident: 10.1016/j.bbagen.2014.01.027_bb0265
  article-title: Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1997.1196
– volume: 11
  start-page: BR266
  year: 2005
  ident: 10.1016/j.bbagen.2014.01.027_bb0160
  article-title: Hydrolysis of myelin basic protein by IgM and IgA antibodies from the sera of patients with multiple sclerosis
  publication-title: Med. Sci. Monit.
– volume: 244
  start-page: 1158
  year: 1989
  ident: 10.1016/j.bbagen.2014.01.027_bb0070
  article-title: Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody
  publication-title: Science
  doi: 10.1126/science.2727702
– volume: 42
  start-page: 14328
  year: 2003
  ident: 10.1016/j.bbagen.2014.01.027_bb0270
  article-title: Degradation of beta-amyloid by proteolytic antibody light chains
  publication-title: Biochemistry
  doi: 10.1021/bi035038d
– volume: 81
  start-page: 191
  year: 2002
  ident: 10.1016/j.bbagen.2014.01.027_bb0115
  article-title: Catalytic diversity of polyclonal RNA-hydrolyzing IgG antibodies from the sera of patients with systemic lupus erythematosus
  publication-title: Immunol. Lett.
  doi: 10.1016/S0165-2478(02)00006-8
– volume: 155
  start-page: 2695
  year: 1995
  ident: 10.1016/j.bbagen.2014.01.027_bb0145
  article-title: Unexpected presence of polyreactive catalytic antibodies in IgG from unimmunized donors and decreased levels in rheumatoid arthritis
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.155.5.2695
– volume: 51
  start-page: 313
  year: 1989
  ident: 10.1016/j.bbagen.2014.01.027_bb0290
  article-title: The role of the human anti-DNA idiotype 16/6 in autoimmunity
  publication-title: Clin. Immunol. Immunopathol.
  doi: 10.1016/0090-1229(89)90030-5
– volume: 7
  start-page: 733
  year: 2011
  ident: 10.1016/j.bbagen.2014.01.027_bb0310
  article-title: Structural modification of DNA—a therapeutic option in SLE?
  publication-title: Nat. Rev. Rheumatol.
  doi: 10.1038/nrrheum.2011.153
– volume: 75
  start-page: 13
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0195
  article-title: Mechanism and functional role of antibody catalysis
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/BF02787705
– volume: 352
  start-page: 624
  year: 1991
  ident: 10.1016/j.bbagen.2014.01.027_bb0335
  article-title: Making antibody fragments using phage display libraries
  publication-title: Nature
  doi: 10.1038/352624a0
– volume: 6
  start-page: 179
  year: 1999
  ident: 10.1016/j.bbagen.2014.01.027_bb0135
  article-title: Antibodies with amylolytic activity
  publication-title: Prot. Pept. Lett.
  doi: 10.1023/A:1008826909441
– volume: 266
  start-page: 15571
  year: 1991
  ident: 10.1016/j.bbagen.2014.01.027_bb0205
  article-title: Vasoactive intestinal peptide hydrolysis by antibody light chains
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)98440-1
– volume: 92
  start-page: 254
  year: 1995
  ident: 10.1016/j.bbagen.2014.01.027_bb0420
  article-title: Cleavage of supercoiled plasmid DNA by autoantibody Fab fragment: application of the flow linear dichroism technique
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.92.1.254
– volume: 269
  start-page: 1835
  year: 1995
  ident: 10.1016/j.bbagen.2014.01.027_bb0015
  article-title: From molecular diversity to catalysis: lessons from the immune system
  publication-title: Science
  doi: 10.1126/science.7569920
– volume: 7
  start-page: 265
  year: 2003
  ident: 10.1016/j.bbagen.2014.01.027_bb0045
  article-title: Catalytic antibodies in healthy humans and patients with autoimmune and viral pathologies
  publication-title: J. Cell. Mol. Med.
  doi: 10.1111/j.1582-4934.2003.tb00227.x
– volume: 3
  start-page: 157
  year: 2012
  ident: 10.1016/j.bbagen.2014.01.027_bb0450
  article-title: Autoantibodies and natural catalytic antibodies in health, multiple sclerosis, and some other diseases
  publication-title: Adv. Neuroimmune Biol.
  doi: 10.3233/NIB-2012-012042
– volume: 12
  start-page: 427
  year: 1987
  ident: 10.1016/j.bbagen.2014.01.027_bb0005
  article-title: Antibodies as enzymes
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/0968-0004(87)90208-8
– volume: 75
  start-page: 3
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0090
  article-title: Antibody catalysis based on functional mimicry
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/BF02787704
– volume: 18
  start-page: 413
  year: 2005
  ident: 10.1016/j.bbagen.2014.01.027_bb0175
  article-title: Casein-hydrolyzing activity of sIgA antibodies from human milk
  publication-title: J. Mol. Recognit.
  doi: 10.1002/jmr.743
– volume: 77
  start-page: 115
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0235
  article-title: Prothrombin cleaving antibody light chains
  publication-title: Chem. Immunol.
  doi: 10.1159/000058801
– volume: 2012
  start-page: 683829
  year: 2012
  ident: 10.1016/j.bbagen.2014.01.027_bb0325
  article-title: Role of structure-based changes due to somatic mutation in highly homologous DNA-binding and DNA-hydrolyzing autoantibodies exemplified by A23P substitution in the VH domain
  publication-title: Autoimmune Dis.
– volume: 75
  start-page: 63
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0225
  article-title: Catalytic DNA- and RNA-hydrolyzing antibodies from milk of healthy human mothers
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/BF02787709
– volume: 73
  start-page: 121
  year: 1995
  ident: 10.1016/j.bbagen.2014.01.027_bb0010
  article-title: Catalytic antibodies: evolution of protein function in real time
  publication-title: EXS
– start-page: 1
  year: 2005
  ident: 10.1016/j.bbagen.2014.01.027_bb0030
– volume: 10
  start-page: 1203
  year: 2010
  ident: 10.1016/j.bbagen.2014.01.027_bb0055
  article-title: Natural catalytic antibodies in norm, autoimmune, viral, and bacterial diseases
  publication-title: Scientific World Journal
  doi: 10.1100/tsw.2010.98
– volume: 63
  start-page: 1239
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0300
  article-title: Polyclonal antibodies from blood and cerebrospinal fluid of patients with multiple sclerosis effectively hydrolyze DNA and RNA
  publication-title: Biochem. Mosc.
– volume: 76
  start-page: 163
  year: 2001
  ident: 10.1016/j.bbagen.2014.01.027_bb0125
  article-title: Catalytic heterogeneity of polyclonal DNA-hydrolyzing antibodies from the sera of patients with multiple sclerosis
  publication-title: Immunol. Lett.
  doi: 10.1016/S0165-2478(01)00185-7
– volume: 103
  start-page: 281
  year: 2006
  ident: 10.1016/j.bbagen.2014.01.027_bb0170
  article-title: Autoantibodies to myelin basic protein catalyze site-specific degradation of their antigen
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0509849103
– volume: 98
  start-page: 1793
  year: 2001
  ident: 10.1016/j.bbagen.2014.01.027_bb0445
  article-title: Anti-DNA antibodies are a major component of the intrathecal B cell response in multiple sclerosis
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.98.4.1793
– volume: 83
  start-page: 85
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0200
  article-title: Does catalytic activity of Bence–Jones proteins contribute to the pathogenesis of multiple myeloma?
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1385/ABAB:83:1-3:85
– volume: 13
  start-page: 289
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0400
  article-title: Removal of catalytic activity by EDTA from antibody light chain
  publication-title: Biometals
  doi: 10.1023/A:1009252200231
– volume: 256
  start-page: 665
  year: 1992
  ident: 10.1016/j.bbagen.2014.01.027_bb0075
  article-title: DNA hydrolyzing autoantibodies
  publication-title: Science
  doi: 10.1126/science.1585181
– volume: 2
  start-page: 405
  year: 2008
  ident: 10.1016/j.bbagen.2014.01.027_bb0385
  article-title: Immunoglobulins from blood of patients with multiple sclerosis like catalytic heterogeneous nucleases
  publication-title: Russ. J. Immunol.
– volume: 1774
  start-page: 884
  year: 2007
  ident: 10.1016/j.bbagen.2014.01.027_bb0345
  article-title: Activation of DNA-hydrolyzing antibodies from the sera of autoimmune-prone MRL-lpr/lpr mice by different metal ions
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbapap.2007.05.006
– volume: 44
  start-page: 37
  year: 1977
  ident: 10.1016/j.bbagen.2014.01.027_bb0435
  article-title: Lessons from a monoclonal antibody to double-stranded DNA
  publication-title: J. Med. Dent. Sci.
– volume: 3
  start-page: 850
  year: 2001
  ident: 10.1016/j.bbagen.2014.01.027_bb0280
  article-title: Immune response to DNA in systemic lupus erythematosus
  publication-title: Isr. Med. Assoc. J.
– volume: 75
  start-page: 45
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0295
  article-title: Novel functional activities of anti-DNA autoantibodies from sera of patients with lymphoproliferative and autoimmune diseases
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/BF02787708
– volume: 61
  start-page: 109
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0095
  article-title: Production and characterization of monoclonal anti-idiotypic antibody exhibiting a catalytic activity similar to carboxypeptidase A
  publication-title: J. Biotechnol.
  doi: 10.1016/S0168-1656(98)00009-1
– volume: 7
  start-page: 65
  year: 1994
  ident: 10.1016/j.bbagen.2014.01.027_bb0375
  article-title: DNA recognition by DNase I
  publication-title: J. Mol. Recognit.
  doi: 10.1002/jmr.300070203
– volume: 86
  start-page: 217
  year: 2004
  ident: 10.1016/j.bbagen.2014.01.027_bb0255
  article-title: Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant
  publication-title: Biotechnol. Bioeng.
  doi: 10.1002/bit.20031
– volume: 14
  start-page: 699
  year: 2010
  ident: 10.1016/j.bbagen.2014.01.027_bb0185
  article-title: Affinity and catalytic heterogeneity of polyclonal myelin basic protein-hydrolyzing IgGs from sera of patients with multiple sclerosis
  publication-title: J. Cell. Mol. Med.
  doi: 10.1111/j.1582-4934.2009.00738.x
– volume: 47
  start-page: 157
  year: 1994
  ident: 10.1016/j.bbagen.2014.01.027_bb0340
  article-title: Selection and rapid purification of murine antibody fragments that bind a transition-state analog by phage display
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/BF02787932
– volume: 10
  start-page: 229
  year: 1993
  ident: 10.1016/j.bbagen.2014.01.027_bb0020
  article-title: Recent developments in catalytic antibodies
  publication-title: Int. Rev. Immunol.
  doi: 10.3109/08830189309061698
– volume: 264
  start-page: 1154
  year: 1996
  ident: 10.1016/j.bbagen.2014.01.027_bb0405
  article-title: Site-directed mutagenesis of the catalytic residues of bovine pancreatic deoxyribonuclease I
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1996.0703
– volume: 20
  start-page: 131
  year: 1978
  ident: 10.1016/j.bbagen.2014.01.027_bb0440
  article-title: Ribonucleic acid in the immune response
  publication-title: Mol. Cell. Biochem.
  doi: 10.1007/BF00243760
– volume: 9
  start-page: 24
  year: 1999
  ident: 10.1016/j.bbagen.2014.01.027_bb0025
  article-title: Opportunities at the interface of chemistry and biology
  publication-title: Trends Cell Biol.
  doi: 10.1016/S0962-8924(99)01682-7
– volume: 63
  start-page: 1239
  year: 1998
  ident: 10.1016/j.bbagen.2014.01.027_bb0120
  article-title: Polyclonal antibodies from blood and cerebrospinal fluid of patients with multiple sclerosis effectively hydrolyze DNA and RNA
  publication-title: Biochemistry (Mosc)
– volume: 34
  start-page: 1083
  year: 1997
  ident: 10.1016/j.bbagen.2014.01.027_bb0315
  article-title: DNA hydrolysis by monoclonal anti-ssDNA autoantibody BV 04-01: origins of catalytic activity
  publication-title: Mol. Immunol.
  doi: 10.1016/S0161-5890(97)00129-6
– volume: 283
  start-page: 899
  year: 2008
  ident: 10.1016/j.bbagen.2014.01.027_bb0250
  article-title: Catalytic features and eradication ability of antibody light-chain UA15-L against Helicobacter pylori
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M705674200
– year: 1985
  ident: 10.1016/j.bbagen.2014.01.027_bb0370
– volume: 21
  start-page: 233
  year: 2008
  ident: 10.1016/j.bbagen.2014.01.027_bb0355
  article-title: Immunization of rabbits with DNase I produces polyclonal antibodies with DNase and RNase activities
  publication-title: J. Mol. Recognit.
  doi: 10.1002/jmr.890
– volume: 276
  start-page: 28314
  year: 2001
  ident: 10.1016/j.bbagen.2014.01.027_bb0330
  article-title: Phosphonate ester probes for proteolytic antibodies
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M102530200
– volume: 83
  start-page: 71
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0240
  article-title: Natural catalytic immunity is not restricted to autoantigenic substrates: identification of a human immunodeficiency virus gp 120-cleaving antibody light chain
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1385/ABAB:83:1-3:71
– volume: 97
  start-page: 13526
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0105
  article-title: Enzyme mimicry by the antiidiotypic antibody approach
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.200360497
– year: 1971
  ident: 10.1016/j.bbagen.2014.01.027_bb0380
  article-title: The Enzymes
– volume: 255
  start-page: 3726
  year: 1980
  ident: 10.1016/j.bbagen.2014.01.027_bb0415
  article-title: The effect of divalent cations on the mode of action of DNase I. The initial reaction products produced from covalently closed circular DNA
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)85765-4
– volume: 23
  start-page: 486
  year: 2010
  ident: 10.1016/j.bbagen.2014.01.027_bb0180
  article-title: IgGs containing light chains of the λ and κ type and of all subclasses (IgG1–IgG4) from sera of patients with multiple sclerosis hydrolyze DNA
  publication-title: J. Mol. Recognit.
  doi: 10.1002/jmr.1016
– start-page: 1
  year: 2010
  ident: 10.1016/j.bbagen.2014.01.027_bb0060
  article-title: Natural catalytic antibodies in norm and in autoimmune diseases
– volume: 90
  start-page: 8876
  year: 1993
  ident: 10.1016/j.bbagen.2014.01.027_bb0100
  article-title: Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: production of a catalytic antibody with a cholinesterase activity
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.90.19.8876
– volume: 6
  start-page: e1001000
  year: 2010
  ident: 10.1016/j.bbagen.2014.01.027_bb0410
  article-title: How cations can assist DNase I in DNA binding and hydrolysis
  publication-title: PLoS Comput. Biol.
  doi: 10.1371/journal.pcbi.1001000
– volume: 14
  start-page: 4529
  year: 2004
  ident: 10.1016/j.bbagen.2014.01.027_bb0275
  article-title: Antibody light chain-catalyzed hydrolysis of a hepatitis C virus peptide
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2004.06.044
– volume: 416
  start-page: 23
  year: 1997
  ident: 10.1016/j.bbagen.2014.01.027_bb0215
  article-title: DNA-hydrolyzing activity of the light chain of IgG antibodies from milk of healthy human mothers
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(97)01163-0
– volume: 39
  start-page: 6459
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0230
  article-title: Monoclonal antibody light chain with prothrombinase activity
  publication-title: Biochemistry
  doi: 10.1021/bi992588w
– volume: 92
  start-page: 2145
  year: 2002
  ident: 10.1016/j.bbagen.2014.01.027_bb0430
  article-title: Unexpectedly high occurrence of catalytic antibodies in MRL/lpr and SJL mice immunized with a transition-state analog: is there a linkage to autoimmunity?
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.92.6.2145
– volume: 269
  start-page: 235
  year: 2002
  ident: 10.1016/j.bbagen.2014.01.027_bb0035
  article-title: Human catalytic RNA- and DNA-hydrolyzing antibodies
  publication-title: J. Immunol. Methods
  doi: 10.1016/S0022-1759(02)00234-X
– volume: 92
  start-page: 545
  year: 2010
  ident: 10.1016/j.bbagen.2014.01.027_bb0390
  article-title: DNA-hydrolyzing activity of IgG antibodies from the sera of patients with tick-borne encephalitis
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2010.01.022
– volume: 8
  start-page: 359
  year: 2004
  ident: 10.1016/j.bbagen.2014.01.027_bb0155
  article-title: Hydrolysis of myelin basic protein by polyclonal catalytic IgGs from the sera of patients with multiple sclerosis
  publication-title: J. Cell. Mol. Med.
  doi: 10.1111/j.1582-4934.2004.tb00325.x
– volume: 1
  start-page: 116
  year: 2007
  ident: 10.1016/j.bbagen.2014.01.027_bb0210
  article-title: A peculiarity of DNA hydrolysis by antibodies from patients with diabetes
  publication-title: Russ. J. Immunol.
– volume: 40
  start-page: 857
  year: 2006
  ident: 10.1016/j.bbagen.2014.01.027_bb0305
  article-title: DNA-hydrolyzing IgG antibodies from the blood of patients with acquired immune deficiency syndrome
  publication-title: Mol. Biol. (Mosk)
  doi: 10.1134/S0026893306050128
– volume: 6
  start-page: 460
  year: 2000
  ident: 10.1016/j.bbagen.2014.01.027_bb0110
  article-title: Catalytic heterogeneity of polyclonal RNA-hydrolyzing IgM from sera of patients with lupus erythematosus
  publication-title: Med. Sci. Monit.
– volume: 17
  start-page: 285
  year: 1988
  ident: 10.1016/j.bbagen.2014.01.027_bb0285
  article-title: Autoimmune diseases other than lupus share common anti-DNA idiotypes
  publication-title: Immunol. Lett.
  doi: 10.1016/0165-2478(88)90043-0
– volume: 20
  start-page: 1031
  year: 2008
  ident: 10.1016/j.bbagen.2014.01.027_bb0360
  article-title: Anti-RNase antibodies against pancreatic ribonuclease A hydrolyze RNA and DNA
  publication-title: Int. Immunol.
  doi: 10.1093/intimm/dxn061
– volume: 103
  start-page: 75
  year: 2006
  ident: 10.1016/j.bbagen.2014.01.027_bb0165
  article-title: Metal-dependent hydrolysis of myelin basic protein by IgGs from the sera of patients with multiple sclerosis
  publication-title: Immunol. Lett.
  doi: 10.1016/j.imlet.2005.10.018
– volume: 28
  start-page: 738
  year: 1994
  ident: 10.1016/j.bbagen.2014.01.027_bb0080
  article-title: Interaction of catalytically active antibodies with oligoribonucleotides
  publication-title: Mol. Biol. (Mosk)
– volume: 24
  start-page: 759
  year: 2012
  ident: 10.1016/j.bbagen.2014.01.027_bb0190
  article-title: IgGs containing light chains of the lambda- and kappa-type and of all subclasses (IgG1–IgG4) from the sera of patients with systemic lupus erythematosus hydrolyze myelin basic protein
  publication-title: Int. Immunol.
  doi: 10.1093/intimm/dxs071
– volume: 270
  start-page: 15257
  year: 1995
  ident: 10.1016/j.bbagen.2014.01.027_bb0150
  article-title: Natural catalytic antibodies: peptide-hydrolyzing activities of Bence Jones proteins and VL fragment
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.270.25.15257
– volume: 22
  start-page: 26
  year: 2009
  ident: 10.1016/j.bbagen.2014.01.027_bb0395
  article-title: Oxidoreductase activities of polyclonal IgGs from the sera of Wistar rats are better activated by combinations of different metal ions
  publication-title: J. Mol. Recognit.
  doi: 10.1002/jmr.923
– volume: 281
  start-page: 15287
  year: 2006
  ident: 10.1016/j.bbagen.2014.01.027_bb0320
  article-title: Heavy and light chain variable single domains of an anti-DNA binding antibody hydrolyze both double- and single-stranded DNAs without sequence specificity
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M600937200
– volume: 47
  start-page: 229
  year: 1994
  ident: 10.1016/j.bbagen.2014.01.027_bb0085
  article-title: Abzyme generation using an anti-idiotypic antibody as the “internal image” of an enzyme active site
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/BF02787937
– volume: 86
  start-page: 291
  year: 2003
  ident: 10.1016/j.bbagen.2014.01.027_bb0140
  article-title: Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis
  publication-title: Immunol. Lett.
  doi: 10.1016/S0165-2478(03)00042-7
– volume: 21
  start-page: 337
  year: 2008
  ident: 10.1016/j.bbagen.2014.01.027_bb0350
  article-title: Antibodies against RNA hydrolyze RNA and DNA
  publication-title: J. Mol. Recognit.
  doi: 10.1002/jmr.906
– volume: 21
  start-page: 349
  year: 2009
  ident: 10.1016/j.bbagen.2014.01.027_bb0365
  article-title: Immunization of rabbits with DNase II leads to formation of polyclonal antibodies with DNase and RNase activities
  publication-title: Int. Immunol.
  doi: 10.1093/intimm/dxp004
SSID ssj0000595
ssj0025309
Score 2.2067316
Snippet DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies. An immunoglobulin light chain phagemid library derived...
DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies.BACKGROUNDDNase antibodies can play an important role in...
DNase antibodies can play an important role in the pathogenesis of different autoimmune pathologies.An immunoglobulin light chain phagemid library derived from...
SourceID proquest
pubmed
crossref
SourceType Aggregation Database
Index Database
Enrichment Source
StartPage 1725
SubjectTerms affinity chromatography
antibodies
Antibody Affinity
bacteriophages
calcium
Catalysis
cations
clones
Cloning, Molecular
cobalt
copper
deoxyribonucleases
Deoxyribonucleases - immunology
divalent metals
DNA
Escherichia coli
gel chromatography
Humans
Hydrogen-Ion Concentration
hydrolysis
Immunoglobulin kappa-Chains - genetics
immunoglobulin light chains
lupus erythematosus
Lupus Erythematosus, Systemic - immunology
lymphocytes
magnesium
Magnesium - pharmacology
manganese
Manganese - pharmacology
molecular cloning
nickel
pathogenesis
patients
potassium chloride
Recombinant Proteins - biosynthesis
sodium chloride
zinc
Title Systemic lupus erythematosus: Molecular cloning of fourteen recombinant DNase monoclonal kappa light chains with different catalytic properties
URI https://www.ncbi.nlm.nih.gov/pubmed/24462577
https://www.proquest.com/docview/1519836900
https://www.proquest.com/docview/2000195406
Volume 1840
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFLbKJsReEIxbuUxG4i1KlXsb3qoBGkzrAyqwt8h2bNGtJFWbTCoP_AX-F7-Kc-w4aRkDRh-iyHZct-eLz8XnQsiLRPosBMbpgrScuhEX8M55kXKDVA6jlIucJRg7fDJJjj5E707j017vx4bXUl3xgfj627iS_6EqtAFdMUr2GpRtJ4UGuAf6whUoDNd_orFJNz4Tzrxe1CtHLtcmB2u5qrWn24mtfeuIuTG7gmioYOYKXbNQF_7CtSeM82oC3MyBhZc4Esh2zhYL5sxRdcfgYHSk0SZbW1AFWtHws8Z8rws06C8r645oj4hnpfg8w2wEjqwcPiuNEYVh-g42sPmunVXN0RTUnSmVWEnkfGZi1d4u4cYZD1qrQV3IC93zkSG_xN5J2zsBLl801mBt7F_bRxu7hh91_lc2nsuLXBAX4-292iR3alC5ufWCJBZvsHF_aJLJXGIRxlpxNuAchmEGXD8yiVuHHUu0bgC_cMrWf9G6xp1lZpYMZ8k8P4NZbpDdAFQW3HMH3zp3IxBjY3OiZX6VDePUvoaX17ItJl2h-2gZaHqH3G6UFzo2SLxLerLYJzdNOdP1Prl1aKsH3iPfLTapxibdwuZL2iKTNsikpaIWmXQDmVQjk3bIpBqZVCOTGmRSRCZtkUlbZNIOmffJ9M3r6eGR2xT_cEUYeZWrRCi9MPU4T3LheSxSsYANhOW-4IEMxYhhZscgDlLlScVVLvmIhQG6eXHBw_AB2SnKQj4iNFBKCRgZM55GozziPGfw4aECVUn4sk9C-1dnokmMj_VZ5tmfyNwnbvvUwiSG-cv455aKGZACj-VYIct6lYHMnY7CJPW8q8cEWhcD7Srpk4cGAu23goCeAOMdPr7mip6Qve69e0p2qmUtn4GEXfEDDd0Dsjs-fv_p-CfLotzb
linkProvider Elsevier
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Systemic+lupus+erythematosus%3A+Molecular+cloning+of+fourteen+recombinant+DNase+monoclonal+kappa+light+chains+with+different+catalytic+properties&rft.jtitle=Biochimica+et+biophysica+acta.+General+subjects&rft.au=Kostrikina%2C+Irina+A.&rft.au=Buneva%2C+Valentina+N.&rft.au=Nevinsky%2C+Georgy+A.&rft.date=2014-06-01&rft.issn=0304-4165&rft.volume=1840&rft.issue=6&rft.spage=1725&rft.epage=1737&rft_id=info:doi/10.1016%2Fj.bbagen.2014.01.027&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_bbagen_2014_01_027
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon