Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigation...
Saved in:
Published in | Journal of molecular biology Vol. 223; no. 4; pp. 1167 - 1169 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Elsevier Ltd
20.02.1992
Elsevier |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The dimeric glucose oxidase from
Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 Å resolution and belong to the orthorhombic space group
P2
12
12
1, with refined lattice constants of
a = 59.3
A
̊
, b = 136.3
A
̊
and
c = 156.7
A
̊
. Assuming two monomers (≈ 135 kDa) per asymmetric unit the
V
m value is 2.3 Å
3/Da. |
---|---|
AbstractList | The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 angstroms resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 angstroms, b = 136.3 angstroms and c = 156.7 angstroms. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 cubic angstroms/Da. The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 A3/Da. The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 A3/Da.The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 A3/Da. The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 Å resolution and belong to the orthorhombic space group P2 12 12 1, with refined lattice constants of a = 59.3 A ̊ , b = 136.3 A ̊ and c = 156.7 A ̊ . Assuming two monomers (≈ 135 kDa) per asymmetric unit the V m value is 2.3 Å 3/Da. The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. |
Author | Hecht, Hans-Jürgen Kalisz, Henryk M. Schmid, Rolf D. Schomburg, Dietmar Hendle, Jörg |
Author_xml | – sequence: 1 givenname: Jörg surname: Hendle fullname: Hendle, Jörg organization: Department of Enzyme Technology GBF-Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany – sequence: 2 givenname: Hans-Jürgen surname: Hecht fullname: Hecht, Hans-Jürgen organization: Department of Molecular Structural Research GBF-Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany – sequence: 3 givenname: Henryk M. surname: Kalisz fullname: Kalisz, Henryk M. organization: Department of Enzyme Technology GBF-Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany – sequence: 4 givenname: Rolf D. surname: Schmid fullname: Schmid, Rolf D. organization: Department of Enzyme Technology GBF-Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany – sequence: 5 givenname: Dietmar surname: Schomburg fullname: Schomburg, Dietmar organization: Department of Molecular Structural Research GBF-Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany |
BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5168077$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/1538394$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkk2LFDEQhhtZWXdX_4FiDiJ6aE06nXTiQZDBL1hWwRW8hZqkMkS7O2PSLY744818sIIH51SEet6qSr11Xp2MccSqus_oM0aZfE5p09SN4vKJbp5q2siuvrpVnTGqdK0kVyfV2Q1ypzrP-SulVPBWnVanTHDFdXtW_V6kTZ6g78MvmEIcCYyOrBP2YQgjpA35UifYEBe8T2B3RJ5mFzCT6AkQh6t-Y2Pe9DChI6t-Lg8k8WdwUKJPcSAfcQw2lBbzQGCAFWT4FnDMeLe67aHPeO8QL6rrN6-vF-_qyw9v3y9eXda2jDmVDyyZ9tahaKHtJC5BOw0gpWu5bQG5F37JvPQKpBPYyU4wcJoxKxTVjF9Uj_dl1yl-nzFPZgjZYt_DiHHOpmsUE0qIo2Crdcs7qo6CTDasZVQW8MEBnJcDOrNOYShbNYf9l_yjQx6yhb7seLQh32CCSUW7rmDtHrMp5pzQ_y1EzfYYzNZps3Xa6MbsjsFcFdmLf2Q2TDubpwShPyZ-uBd7iAZWqYz1-VNDGaesa7Xg26le7gks3v0ImEy2xVeLLiS0k3Ex_L_FH3Yx2PM |
CODEN | JMOBAK |
CitedBy_id | crossref_primary_10_1111_j_1432_1033_1996_0340u_x crossref_primary_10_1295_polymj_30_350 crossref_primary_10_1016_j_eurpolymj_2006_11_029 crossref_primary_10_1016_j_pep_2005_06_003 crossref_primary_10_1016_S0003_9861_03_00127_9 crossref_primary_10_1295_polymj_31_274 crossref_primary_10_1016_j_eurpolymj_2014_11_017 crossref_primary_10_1016_S0141_0229_96_00004_X crossref_primary_10_1128_AEM_64_4_1405_1411_1998 |
Cites_doi | 10.1016/S0022-2836(05)80179-2 10.1016/0021-9673(90)85049-2 10.1016/0022-2836(68)90205-2 10.1271/bbb1961.39.1803 10.1016/0006-3002(60)91406-2 10.1021/bi00892a018 10.1016/0014-5793(89)81061-0 10.1016/S0021-9258(19)39664-4 10.1016/0005-2744(76)90221-7 10.1107/S0021889887086436 10.1016/S0021-9673(01)85007-X |
ContentType | Journal Article |
Copyright | 1992 1992 INIST-CNRS |
Copyright_xml | – notice: 1992 – notice: 1992 INIST-CNRS |
DBID | FBQ AAYXX CITATION IQODW CGR CUY CVF ECM EIF NPM 7QL 8FD C1K FR3 M7N M81 P64 7S9 L.6 7X8 |
DOI | 10.1016/0022-2836(92)90267-N |
DatabaseName | AGRIS CrossRef Pascal-Francis Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Bacteriology Abstracts (Microbiology B) Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database Algology Mycology and Protozoology Abstracts (Microbiology C) Biochemistry Abstracts 3 Biotechnology and BioEngineering Abstracts AGRICOLA AGRICOLA - Academic MEDLINE - Academic |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Technology Research Database Biochemistry Abstracts 3 Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) Engineering Research Database Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management AGRICOLA AGRICOLA - Academic MEDLINE - Academic |
DatabaseTitleList | AGRICOLA MEDLINE MEDLINE - Academic Technology Research Database |
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 – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Biology |
EISSN | 1089-8638 |
EndPage | 1169 |
ExternalDocumentID | 1538394 5168077 10_1016_0022_2836_92_90267_N US201301749537 002228369290267N |
Genre | Journal Article |
GroupedDBID | --- --K --M -DZ -ET -~X .55 .GJ .~1 0R~ 186 1B1 1RT 1~. 1~5 29L 3O- 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 85S 8P~ 9JM AAAJQ AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AARKO AAXUO ABEFU ABFNM ABFRF ABGSF ABJNI ABLJU ABMAC ABOCM ABPPZ ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACKIV ACNCT ACRLP ADBBV ADEZE ADFGL ADIYS ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFFNX AFKWA AFMIJ AFTJW AFXIZ AGEKW AGHFR AGRDE AGUBO AGYEJ AHHHB AHPSJ AI. AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CAG CJTIS COF CS3 DM4 DOVZS DU5 EBS EFBJH EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q G8K GBLVA GX1 HLW HMG HVGLF HX~ HZ~ H~9 IH2 IHE J1W K-O KOM LG5 LUGTX LX2 LZ5 M41 MO0 MVM N9A NEJ O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG RNS ROL RPZ SBG SDF SDG SDP SES SEW SIN SPCBC SSI SSU SSZ T5K TWZ UQL VH1 VQA WH7 WUQ X7M XJT XOL XPP Y6R YQT YYP ZGI ZKB ZMT ZU3 ~G- ~KM ABPIF ABPTK AEQTP FBQ AAHBH AATTM AAXKI AAYWO AAYXX ABDPE ABWVN ACRPL ACVFH ADCNI ADNMO ADVLN ADXHL AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH EFKBS IQODW CGR CUY CVF ECM EIF NPM PKN 7QL 8FD C1K FR3 M7N M81 P64 7S9 L.6 7X8 |
ID | FETCH-LOGICAL-c538t-28b19fcde54a476eba9d9aa66d43c4ae3f5fb1f6f8a6d5e76751ad911c580913 |
ISSN | 0022-2836 |
IngestDate | Fri Jul 11 01:59:10 EDT 2025 Thu Jul 10 18:05:43 EDT 2025 Fri Jul 11 15:09:29 EDT 2025 Wed Feb 19 02:32:48 EST 2025 Mon Jul 21 09:14:44 EDT 2025 Thu Apr 24 22:50:49 EDT 2025 Tue Jul 01 03:27:55 EDT 2025 Wed Dec 27 19:23:27 EST 2023 Fri Feb 23 02:33:35 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 4 |
Keywords | crystallization Penicillium amagasakiense glucose oxidase Fungi Glucose oxidase Unit cell Purification Enzyme Crystallization Coenzyme enzyme complex Fungi Imperfecti X ray diffraction Thallophyta |
Language | English |
License | https://www.elsevier.com/tdm/userlicense/1.0 CC BY 4.0 |
LinkModel | OpenURL |
MergedId | FETCHMERGED-LOGICAL-c538t-28b19fcde54a476eba9d9aa66d43c4ae3f5fb1f6f8a6d5e76751ad911c580913 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 1538394 |
PQID | 16214106 |
PQPubID | 23462 |
PageCount | 3 |
ParticipantIDs | proquest_miscellaneous_72815855 proquest_miscellaneous_49943708 proquest_miscellaneous_16214106 pubmed_primary_1538394 pascalfrancis_primary_5168077 crossref_primary_10_1016_0022_2836_92_90267_N crossref_citationtrail_10_1016_0022_2836_92_90267_N fao_agris_US201301749537 elsevier_sciencedirect_doi_10_1016_0022_2836_92_90267_N |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 1900 |
PublicationDate | 1992-02-20 |
PublicationDateYYYYMMDD | 1992-02-20 |
PublicationDate_xml | – month: 02 year: 1992 text: 1992-02-20 day: 20 |
PublicationDecade | 1990 |
PublicationPlace | Oxford |
PublicationPlace_xml | – name: Oxford – name: England |
PublicationTitle | Journal of molecular biology |
PublicationTitleAlternate | J Mol Biol |
PublicationYear | 1992 |
Publisher | Elsevier Ltd Elsevier |
Publisher_xml | – name: Elsevier Ltd – name: Elsevier |
References | Kriechbaum, Heilmann, Wientjes, Hahn, Jany, Gassen, Sharif, Alaeddinoglu (BIB11) 1989; 255 Nakamatsu, Akamatsu, Miyajima, Shiio (BIB15) 1975; 39 (BIB19) 1987 Schmid, Karube (BIB18) 1988; vol. 6b Röhr, Kubicek, Kominek (BIB17) 1983; vol. 3 Kalisz, Hendle, Schmid (BIB10) 1990; 521 Kusai, Sekuzu, Hagihara, Okunuki, Yamauchi, Nakai (BIB12) 1960; 40 Blundell, Johnson (BIB2) 1976 Abalikhina, Morozkin, Bogdanov, Kaverzneva (BIB1) 1971; 36 Matthews (BIB14) 1968; 33 Bright, Porter (BIB3) 1975; vol. 12 Howard, Gilliland, Finzel, Poulos (BIB8) 1987; 20 Eriksson, Kourteva, Yao, Liao, Kilar, Hjerten (BIB5) 1987; 397 Hayashi, Nakamura (BIB7) 1976; 438 Crueger, Creuger (BIB4) 1984; vol. 6a Pazur, Kleppe (BIB16) 1964; 3 Kalisz, Hecht, Schomburg, Schmid (BIB9) 1990; 213 McPherson (BIB13) 1982 Frederick, Tung, Emerick, Masiarz, Chamberlain, Vasavada, Rosenberg, Chakraborty, Schopter, Massey (BIB6) 1990; 265 Frederick (10.1016/0022-2836(92)90267-N_BIB6) 1990; 265 (10.1016/0022-2836(92)90267-N_BIB19) 1987 McPherson (10.1016/0022-2836(92)90267-N_BIB13) 1982 Kalisz (10.1016/0022-2836(92)90267-N_BIB9) 1990; 213 Blundell (10.1016/0022-2836(92)90267-N_BIB2) 1976 Hayashi (10.1016/0022-2836(92)90267-N_BIB7) 1976; 438 Howard (10.1016/0022-2836(92)90267-N_BIB8) 1987; 20 Abalikhina (10.1016/0022-2836(92)90267-N_BIB1) 1971; 36 Kriechbaum (10.1016/0022-2836(92)90267-N_BIB11) 1989; 255 Röhr (10.1016/0022-2836(92)90267-N_BIB17) 1983; vol. 3 Bright (10.1016/0022-2836(92)90267-N_BIB3) 1975; vol. 12 Nakamatsu (10.1016/0022-2836(92)90267-N_BIB15) 1975; 39 Kusai (10.1016/0022-2836(92)90267-N_BIB12) 1960; 40 Crueger (10.1016/0022-2836(92)90267-N_BIB4) 1984; vol. 6a Eriksson (10.1016/0022-2836(92)90267-N_BIB5) 1987; 397 Pazur (10.1016/0022-2836(92)90267-N_BIB16) 1964; 3 Matthews (10.1016/0022-2836(92)90267-N_BIB14) 1968; 33 Schmid (10.1016/0022-2836(92)90267-N_BIB18) 1988; vol. 6b Kalisz (10.1016/0022-2836(92)90267-N_BIB10) 1990; 521 |
References_xml | – year: 1987 ident: BIB19 publication-title: Biosensors-Fundamentals and Applications – start-page: 82 year: 1982 end-page: 159 ident: BIB13 publication-title: Preparation and Analysis of Protein Crystal – volume: vol. 3 start-page: 455 year: 1983 end-page: 465 ident: BIB17 publication-title: Biotechnology – volume: 265 start-page: 3793 year: 1990 end-page: 3802 ident: BIB6 article-title: Glucose oxidase from publication-title: J. Biol. Chem – volume: 397 start-page: 239 year: 1987 end-page: 249 ident: BIB5 article-title: Application of high-performance chromatographic and electrophoretic methods to the purification and characterization of glucose oxidase and catalase from publication-title: J. Chromatogr – volume: 39 start-page: 1803 year: 1975 end-page: 1811 ident: BIB15 article-title: Microbial production of glucose oxidase publication-title: Agric. Biol. Chem – volume: 36 start-page: 191 year: 1971 end-page: 198 ident: BIB1 article-title: Composition and structure of glucose oxidase from publication-title: Biokhimiya – volume: 20 start-page: 383 year: 1987 end-page: 387 ident: BIB8 article-title: The use of imaging proportional counter in macromolecular crystallography publication-title: J. Appl. Crystallogr – volume: 213 start-page: 207 year: 1990 end-page: 209 ident: BIB9 article-title: Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from publication-title: J. Mol. Biol – volume: 40 start-page: 555 year: 1960 end-page: 557 ident: BIB12 article-title: Crystallization of glucose oxidase from publication-title: Biochim. Biophys. Acta – volume: 255 start-page: 63 year: 1989 end-page: 66 ident: BIB11 article-title: Cloning and DNA sequence analysis of the glucose oxidase gene from publication-title: FEBS Letters – volume: vol. 12 start-page: 421 year: 1975 end-page: 505 ident: BIB3 publication-title: The Enzymes – start-page: 59 year: 1976 end-page: 82 ident: BIB2 publication-title: Protein Crystallography – volume: vol. 6a start-page: 421 year: 1984 end-page: 457 ident: BIB4 publication-title: Biotechnology – volume: 438 start-page: 37 year: 1976 end-page: 48 ident: BIB7 article-title: Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies publication-title: Biochim. Biophys. Acta – volume: 521 start-page: 245 year: 1990 end-page: 250 ident: BIB10 article-title: Purification of the glycoprotein glucose oxidase from publication-title: J. Chromatogr – volume: 3 start-page: 578 year: 1964 end-page: 583 ident: BIB16 article-title: The oxidation of glucose and related compounds by glucose oxidase from publication-title: Biochemistry – volume: 33 start-page: 491 year: 1968 end-page: 497 ident: BIB14 article-title: Solvent content of protein crystals publication-title: J. Mol. Biol – volume: vol. 6b start-page: 317 year: 1988 end-page: 365 ident: BIB18 publication-title: Biotechnology – volume: 213 start-page: 207 year: 1990 ident: 10.1016/0022-2836(92)90267-N_BIB9 article-title: Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger publication-title: J. Mol. Biol doi: 10.1016/S0022-2836(05)80179-2 – volume: 521 start-page: 245 year: 1990 ident: 10.1016/0022-2836(92)90267-N_BIB10 article-title: Purification of the glycoprotein glucose oxidase from Penicillium amagasakiense by high-performance liquid chromatography publication-title: J. Chromatogr doi: 10.1016/0021-9673(90)85049-2 – volume: 33 start-page: 491 year: 1968 ident: 10.1016/0022-2836(92)90267-N_BIB14 article-title: Solvent content of protein crystals publication-title: J. Mol. Biol doi: 10.1016/0022-2836(68)90205-2 – volume: 39 start-page: 1803 year: 1975 ident: 10.1016/0022-2836(92)90267-N_BIB15 article-title: Microbial production of glucose oxidase publication-title: Agric. Biol. Chem doi: 10.1271/bbb1961.39.1803 – volume: 40 start-page: 555 year: 1960 ident: 10.1016/0022-2836(92)90267-N_BIB12 article-title: Crystallization of glucose oxidase from Penicillium amagasakiense publication-title: Biochim. Biophys. Acta doi: 10.1016/0006-3002(60)91406-2 – volume: 3 start-page: 578 year: 1964 ident: 10.1016/0022-2836(92)90267-N_BIB16 article-title: The oxidation of glucose and related compounds by glucose oxidase from Aspergillus niger publication-title: Biochemistry doi: 10.1021/bi00892a018 – start-page: 82 year: 1982 ident: 10.1016/0022-2836(92)90267-N_BIB13 – volume: 255 start-page: 63 year: 1989 ident: 10.1016/0022-2836(92)90267-N_BIB11 article-title: Cloning and DNA sequence analysis of the glucose oxidase gene from Aspergillus niger NRRL-3 publication-title: FEBS Letters doi: 10.1016/0014-5793(89)81061-0 – start-page: 59 year: 1976 ident: 10.1016/0022-2836(92)90267-N_BIB2 – volume: 265 start-page: 3793 year: 1990 ident: 10.1016/0022-2836(92)90267-N_BIB6 article-title: Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived enzyme publication-title: J. Biol. Chem doi: 10.1016/S0021-9258(19)39664-4 – volume: vol. 3 start-page: 455 year: 1983 ident: 10.1016/0022-2836(92)90267-N_BIB17 – volume: 438 start-page: 37 year: 1976 ident: 10.1016/0022-2836(92)90267-N_BIB7 article-title: Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2744(76)90221-7 – volume: vol. 12 start-page: 421 year: 1975 ident: 10.1016/0022-2836(92)90267-N_BIB3 – volume: 36 start-page: 191 year: 1971 ident: 10.1016/0022-2836(92)90267-N_BIB1 article-title: Composition and structure of glucose oxidase from Penicillium vitale publication-title: Biokhimiya – volume: 20 start-page: 383 year: 1987 ident: 10.1016/0022-2836(92)90267-N_BIB8 article-title: The use of imaging proportional counter in macromolecular crystallography publication-title: J. Appl. Crystallogr doi: 10.1107/S0021889887086436 – year: 1987 ident: 10.1016/0022-2836(92)90267-N_BIB19 – volume: 397 start-page: 239 year: 1987 ident: 10.1016/0022-2836(92)90267-N_BIB5 article-title: Application of high-performance chromatographic and electrophoretic methods to the purification and characterization of glucose oxidase and catalase from Penicillium chrysogenum publication-title: J. Chromatogr doi: 10.1016/S0021-9673(01)85007-X – volume: vol. 6b start-page: 317 year: 1988 ident: 10.1016/0022-2836(92)90267-N_BIB18 – volume: vol. 6a start-page: 421 year: 1984 ident: 10.1016/0022-2836(92)90267-N_BIB4 |
SSID | ssj0005348 |
Score | 1.4739305 |
Snippet | The dimeric glucose oxidase from
Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation... The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and... The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation... The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. |
SourceID | proquest pubmed pascalfrancis crossref fao elsevier |
SourceType | Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 1167 |
SubjectTerms | Biological and medical sciences crystal structure Crystalline structure crystallization Crystallography crystals dimensions enzymology FAD Fundamental and applied biological sciences. Psychology glucose oxidase Glucose Oxidase - ultrastructure interaction Molecular biophysics Penicillium Penicillium - enzymology Penicillium amagasakiense Protein Conformation purification Structure in molecular biology ultrastructure X-ray crystallography X-Ray Diffraction |
Title | Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense |
URI | https://dx.doi.org/10.1016/0022-2836(92)90267-N https://www.ncbi.nlm.nih.gov/pubmed/1538394 https://www.proquest.com/docview/16214106 https://www.proquest.com/docview/49943708 https://www.proquest.com/docview/72815855 |
Volume | 223 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fb9MwELa6IQQvCAbTCgz8ABJoCmscx0keUbVRwShIdFLfLMd2SqU2Qf0hkYk_nnPsNClaVeAlqtw4rfx98Z3t7-4QegVWVTCZSFjkhKlHwaH2RKhSL9BRpirVYnV6_nnIBtf04zgcdzpZS7W0XqXv5M2tcSX_gyq0Aa4mSvYfkN08FBrgM-ALV0AYrn-FcX9RgnM3m7lYyjrof1ZV6lqUZ2NvIcqqBsrClQRfWtmgjYpUejIrZbEsZ8L4nbV6vfg5VWDbbOTJV51PpdmTMSLmuZiIJbicsPTdVhA1Xu28Lrd75tI7NZutJp3D1kHUQEu7MTBo2j6ZhIw3trEpdSy_z6dWGeQUysoF7pEq7rvXnnuJCQS36U7quZfYYGNHMtqaSc350K1TvN1t2DwN_PCEvDZGlcCUnzdmrT7KH37hl9dXV3x0MR4doDsElhOm0sWHcUsKFNC4zipvnlmHWPrsfNP2JiFv3W_scmEOMlEYba1YwuuV2boouxculQMzeogeOIzwe0ujR6ij8yN019YiLY_QvX5d-u8x-vUHsTAQC7eIhSti4RaxsCMWLjIs8DaxsCMWdsTChli4RSy8RawnaHR5MeoPPFemw5NgLVcwOqmfZFLpkAoaMZ2KRCVCMKZoIKnQQRZmqZ-xLBZMhdpkD_KFAiMrw9hkpT1Gh3mR6xOEewk457FWCdXgKJu1OGUihv6-imiaki4K6oHn0qWwN5VUZrzWKhq4uIGLJ4RXcPFhF3mbXj9sCpc990c1pty5oda95EDBPT1PgAJcTMA-8-tvxKgCYMWfhEHURadbvNj8k9BncS-C71_WPOEAtjm1E7ku1kvuM2K02Gz3HTBQNIh68e47IhL7YRyGXXRsKdgMBEAYJPTp3q7P0P3mrX6ODleLtT4Ff3yVvqhept_LGt4M |
linkProvider | Geneva Foundation for Medical Education and Research |
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=Crystallization+and+preliminary+X-ray+diffraction+studies+of+a+deglycosylated+glucose+oxidase+from+Penicillium+amagasakiense&rft.jtitle=Journal+of+molecular+biology&rft.au=Hendle%2C+J&rft.au=Hecht%2C+H+J&rft.au=Kalisz%2C+H+M&rft.au=Schmid%2C+R+D&rft.date=1992-02-20&rft.issn=0022-2836&rft.volume=223&rft.issue=4&rft.spage=1167&rft_id=info:doi/10.1016%2F0022-2836%2892%2990267-n&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-2836&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-2836&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-2836&client=summon |