Validation of Immunodetection (ELISA) of Ricin Using a Biological Activity Assay

:  The suitability of enzyme‐linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 °C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity...

Full description

Saved in:
Bibliographic Details
Published inJournal of food science Vol. 76; no. 1; pp. C112 - C116
Main Authors Lumor, Stephen E., Hutt, Aaron, Ronningen, Ian, Diez-Gonzalez, Francisco, Labuza, Theodore P.
Format Journal Article
LanguageEnglish
Published Malden, USA Blackwell Publishing Inc 01.01.2011
Wiley
Wiley Subscription Services, Inc
Subjects
activation energy
Adenine - metabolism
Assaying
Biological
biological activity assay
Biological and medical sciences
Chemical Warfare Agents - analysis
Chemical Warfare Agents - toxicity
correlation
DNA - metabolism
ELISA
Enzyme-Linked Immunosorbent Assay
Enzymes
Food Contamination
Food industries
Food Inspection - methods
Food science
Foods
Fundamental and applied biological sciences. Psychology
Half-Life
Hot Temperature
Kinetics
Protein Stability
Proteins
ricin
Ricin - analysis
Ricin - toxicity
Toxicity
Toxins
Toxins, Biological - analysis
Toxins, Biological - toxicity
Validation studies
Validation
Correlation
ricin
biological activity assay
Enzyme immunoassay
Detection
Activation energy
ELISA assay
Biological activity
Immunological method
ELISA
Online AccessGet full text

Cover

Abstract :  The suitability of enzyme‐linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 °C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity (amount of adenine released from DNA) was determined by means of a biological activity assay (BAA). Results showed that inactivation of ricin followed 1st‐order kinetics. The half‐life values for loss of bioactivity at 80, 85, and 90 °C were 1.93, 0.65, and 0.41 min, respectively. Similarly, the half‐life values for reduction in ricin concentration determined by ELISA were 3.06, 0.79, and 0.43 min, respectively. The half‐lives determined by both assays were only significantly different at 80 °C. The Z, Q10, and Arrhenius activation energy values determined by both assays were dissimilar: 11.74 ˚C, 7.12 and 50.1 kcal/mol, respectively, by ELISA; and 14.87 °C, 4.71 and 39.5 kcal/mol, respectively, by BAA. Nevertheless, our findings indicate that the 2 assays were highly correlated (R2= 1), and it can be concluded that ELISA would be a reliable method for detecting residual toxicity of heat‐treated ricin based on fraction lost. Practical Application:  The results of this study indicate that immunodetection, even though not a direct measurement of the biological activity of ricin, is suitable for determining the residual bioactivity of ricin since immunodetection and the biological activity assay used in this investigation were highly correlated. Therefore, ELISA can be used for routine assessment of residual activity or toxicity of ricin in thermally treated foods.
AbstractList The suitability of enzyme-linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 degree C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity (amount of adenine released from DNA) was determined by means of a biological activity assay (BAA). Results showed that inactivation of ricin followed 1st-order kinetics. The half-life values for loss of bioactivity at 80, 85, and 90 degree C were 1.93, 0.65, and 0.41 min, respectively. Similarly, the half-life values for reduction in ricin concentration determined by ELISA were 3.06, 0.79, and 0.43 min, respectively. The half-lives determined by both assays were only significantly different at 80 degree C. The Z, Q10, and Arrhenius activation energy values determined by both assays were dissimilar: 11.74 [ring]C, 7.12 and 50.1 kcal/mol, respectively, by ELISA; and 14.87 degree C, 4.71 and 39.5 kcal/mol, respectively, by BAA. Nevertheless, our findings indicate that the 2 assays were highly correlated (R2= 1), and it can be concluded that ELISA would be a reliable method for detecting residual toxicity of heat-treated ricin based on fraction lost. Practical Application: The results of this study indicate that immunodetection, even though not a direct measurement of the biological activity of ricin, is suitable for determining the residual bioactivity of ricin since immunodetection and the biological activity assay used in this investigation were highly correlated. Therefore, ELISA can be used for routine assessment of residual activity or toxicity of ricin in thermally treated foods.
:  The suitability of enzyme‐linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 °C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity (amount of adenine released from DNA) was determined by means of a biological activity assay (BAA). Results showed that inactivation of ricin followed 1st‐order kinetics. The half‐life values for loss of bioactivity at 80, 85, and 90 °C were 1.93, 0.65, and 0.41 min, respectively. Similarly, the half‐life values for reduction in ricin concentration determined by ELISA were 3.06, 0.79, and 0.43 min, respectively. The half‐lives determined by both assays were only significantly different at 80 °C. The Z, Q10, and Arrhenius activation energy values determined by both assays were dissimilar: 11.74 ˚C, 7.12 and 50.1 kcal/mol, respectively, by ELISA; and 14.87 °C, 4.71 and 39.5 kcal/mol, respectively, by BAA. Nevertheless, our findings indicate that the 2 assays were highly correlated (R2= 1), and it can be concluded that ELISA would be a reliable method for detecting residual toxicity of heat‐treated ricin based on fraction lost. Practical Application:  The results of this study indicate that immunodetection, even though not a direct measurement of the biological activity of ricin, is suitable for determining the residual bioactivity of ricin since immunodetection and the biological activity assay used in this investigation were highly correlated. Therefore, ELISA can be used for routine assessment of residual activity or toxicity of ricin in thermally treated foods.
The suitability of enzyme-linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 °C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity (amount of adenine released from DNA) was determined by means of a biological activity assay (BAA). Results showed that inactivation of ricin followed 1st-order kinetics. The half-life values for loss of bioactivity at 80, 85, and 90 °C were 1.93, 0.65, and 0.41 min, respectively. Similarly, the half-life values for reduction in ricin concentration determined by ELISA were 3.06, 0.79, and 0.43 min, respectively. The half-lives determined by both assays were only significantly different at 80 °C. The Z, Q(10), and Arrhenius activation energy values determined by both assays were dissimilar: 11.74 ˚C, 7.12 and 50.1 kcal/mol, respectively, by ELISA; and 14.87 °C, 4.71 and 39.5 kcal/mol, respectively, by BAA. Nevertheless, our findings indicate that the 2 assays were highly correlated (R(2) = 1), and it can be concluded that ELISA would be a reliable method for detecting residual toxicity of heat-treated ricin based on fraction lost. Practical Application: The results of this study indicate that immunodetection, even though not a direct measurement of the biological activity of ricin, is suitable for determining the residual bioactivity of ricin since immunodetection and the biological activity assay used in this investigation were highly correlated. Therefore, ELISA can be used for routine assessment of residual activity or toxicity of ricin in thermally treated foods.
The suitability of enzyme-linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 ...C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity (amount of adenine released from DNA) was determined by means of a biological activity assay (BAA). Results showed that inactivation of ricin followed 1st-order kinetics. The half-life values for loss of bioactivity at 80, 85, and 90 ...C were 1.93, 0.65, and 0.41 min, respectively. Similarly, the half-life values for reduction in ricin concentration determined by ELISA were 3.06, 0.79, and 0.43 min, respectively. The half-lives determined by both assays were only significantly different at 80 ...C. The Z, Q..., and Arrhenius activation energy values determined by both assays were dissimilar: 11.74 ...C, 7.12 and 50.1 kcal/mol, respectively, by ELISA; and 14.87 ...C, 4.71 and 39.5 kcal/mol, respectively, by BAA. Nevertheless, our findings indicate that the 2 assays were highly correlated (R... = 1), and it can be concluded that ELISA would be a reliable method for detecting residual toxicity of heat-treated ricin based on fraction lost. (ProQuest: ... denotes formulae/symbols omitted.)
The suitability of enzyme‐linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally treated at 80 to 90 °C for up to 9 min, and its residual concentration was determined by means of a commercial ELISA kit, and its bioactivity (amount of adenine released from DNA) was determined by means of a biological activity assay (BAA). Results showed that inactivation of ricin followed 1st‐order kinetics. The half‐life values for loss of bioactivity at 80, 85, and 90 °C were 1.93, 0.65, and 0.41 min, respectively. Similarly, the half‐life values for reduction in ricin concentration determined by ELISA were 3.06, 0.79, and 0.43 min, respectively. The half‐lives determined by both assays were only significantly different at 80 °C. The Z , Q 10 , and Arrhenius activation energy values determined by both assays were dissimilar: 11.74 ˚C, 7.12 and 50.1 kcal/mol, respectively, by ELISA; and 14.87 °C, 4.71 and 39.5 kcal/mol, respectively, by BAA. Nevertheless, our findings indicate that the 2 assays were highly correlated ( R 2 = 1), and it can be concluded that ELISA would be a reliable method for detecting residual toxicity of heat‐treated ricin based on fraction lost. Practical Application:  The results of this study indicate that immunodetection, even though not a direct measurement of the biological activity of ricin, is suitable for determining the residual bioactivity of ricin since immunodetection and the biological activity assay used in this investigation were highly correlated. Therefore, ELISA can be used for routine assessment of residual activity or toxicity of ricin in thermally treated foods.
Author Diez-Gonzalez, Francisco
Lumor, Stephen E.
Hutt, Aaron
Ronningen, Ian
Labuza, Theodore P.
Author_xml – sequence: 1
  givenname: Stephen E.
  surname: Lumor
  fullname: Lumor, Stephen E.
  email: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza ( tplabuza@umn.edu).
  organization: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza (E-mail: tplabuza@umn.edu)
– sequence: 2
  givenname: Aaron
  surname: Hutt
  fullname: Hutt, Aaron
  email: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza ( tplabuza@umn.edu).
  organization: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza (E-mail: tplabuza@umn.edu)
– sequence: 3
  givenname: Ian
  surname: Ronningen
  fullname: Ronningen, Ian
  email: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza ( tplabuza@umn.edu).
  organization: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza (E-mail: tplabuza@umn.edu)
– sequence: 4
  givenname: Francisco
  surname: Diez-Gonzalez
  fullname: Diez-Gonzalez, Francisco
  email: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza ( tplabuza@umn.edu).
  organization: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza (E-mail: tplabuza@umn.edu)
– sequence: 5
  givenname: Theodore P.
  surname: Labuza
  fullname: Labuza, Theodore P.
  email: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza ( tplabuza@umn.edu).
  organization: Authors are with Dept. of Food Science and Nutrition, Univ. of Minnesota, 1334 Eckles Ave., Saint Paul, MN 55108, U.S.A. Direct inquiries to author Labuza (E-mail: tplabuza@umn.edu)
BackLink http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23843523$$DView record in Pascal Francis
https://www.ncbi.nlm.nih.gov/pubmed/21535638$$D View this record in MEDLINE/PubMed
BookMark eNqNkU1v1DAQhi1URLeFv4AiJEQ5ZPG3nQvS0i8WraC0tD1ajuNUXhK7xAns_nuc7rJIHFB9sWfmmVeeeQ_Ang_eApAhOEXpvFtOkWAwJ5KiKYYpC1FByXT1BEx2hT0wgRDjHCEq9sFBjEs4xoQ_A_sYMcI4kRNwcaMbV-neBZ-FOpu37eBDZXtrHlJHp4v51eztWLp0xvnsOjp_l-nsgwtNuHNGN9ksoT9dv85mMer1c_C01k20L7b3Ibg-O_12_DFffDmfH88WuWG4ILlktS6sMdYKY0puJNcWYyMtN6XWlDJW11RTVBskLaFFqeuiZBxWBBW2Ipwcgjcb3fsu_Bhs7FXrorFNo70NQ1SSUyEFw-wRZNpGQcRIHv2XREJAQqHAIqGv_kGXYeh8mljJtNsCIz5CcgOZLsTY2Vrdd67V3VohqEYj1VKNfqnRLzUaqR6MVKvU-nKrP5StrXaNf5xLwOstoGNyoe60Ny7-5ZIkYZgk7v2G--Uau370B9Sns5Or8ZkE8o2Ai71d7QR0912lEQVTt5_P1Q28OLmF6Ku6JL8BjwLIBA
CODEN JFDSAZ
CitedBy_id crossref_primary_10_1021_acs_jproteome_0c00458
crossref_primary_10_1016_j_toxicon_2013_01_005
crossref_primary_10_1080_09540105_2012_753515
crossref_primary_10_1089_bsp_2013_0053
crossref_primary_10_3390_toxins3101332
crossref_primary_10_4315_0362_028X_JFP_11_372
crossref_primary_10_1111_j_1750_3841_2012_02627_x
crossref_primary_10_1021_acs_analchem_6b01486
Cites_doi 10.1016/S0021-9258(18)47538-2
10.1021/ed061p348
10.1128/AEM.00096-06
10.1016/j.jim.2005.01.008
10.1016/j.chroma.2006.08.078
10.1093/nar/26.18.4306
10.1016/S0040-4039(01)96762-0
10.1021/jf061199n
10.1038/249627a0
10.1016/S0015-7368(88)72840-6
10.1093/nar/25.3.518
10.1016/S0015-7368(86)72516-4
10.1007/BF02401711
10.1021/ac8026433
10.1016/S0006-291X(72)80181-5
10.1128/AAC.28.2.265
10.1021/ac061498b
10.1111/j.1365-2621.1979.tb03472.x
10.1042/bj2590639
10.1093/oxfordjournals.jbchem.a022827
10.1016/0041-0101(80)90088-4
ContentType Journal Article
Copyright 2010 Institute of Food Technologists
2015 INIST-CNRS
Copyright Institute of Food Technologists Jan/Feb 2011
Copyright_xml – notice: 2010 Institute of Food Technologists
– notice: 2015 INIST-CNRS
– notice: Copyright Institute of Food Technologists Jan/Feb 2011
DBID BSCLL
IQODW
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QO
7QR
7ST
7T7
7U7
8FD
C1K
F28
FR3
P64
RC3
SOI
7X8
DOI 10.1111/j.1750-3841.2010.01943.x
DatabaseName Istex
Pascal-Francis
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Biotechnology Research Abstracts
Chemoreception Abstracts
Environment Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
Toxicology Abstracts
Technology Research Database
Environmental Sciences and Pollution Management
ANTE: Abstracts in New Technology & Engineering
Engineering Research Database
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
Environment Abstracts
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Genetics Abstracts
Biotechnology Research Abstracts
Technology Research Database
Toxicology Abstracts
Chemoreception Abstracts
Engineering Research Database
Industrial and Applied Microbiology Abstracts (Microbiology A)
Environment Abstracts
ANTE: Abstracts in New Technology & Engineering
Biotechnology and BioEngineering Abstracts
Environmental Sciences and Pollution Management
MEDLINE - Academic
DatabaseTitleList Technology Research Database

MEDLINE
MEDLINE - Academic
Genetics Abstracts
Technology Research Database
CrossRef
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 Economics
EISSN 1750-3841
EndPage C116
ExternalDocumentID 2275088061
10_1111_j_1750_3841_2010_01943_x
21535638
23843523
JFDS1943
ark_67375_WNG_V0PDW01Q_R
Genre article
Validation Studies
Research Support, U.S. Gov't, Non-P.H.S
Journal Article
Feature
GroupedDBID ---
-~X
.3N
.DC
.GA
.GJ
.Y3
05W
0R~
10A
1OB
1OC
29K
3-9
31~
33P
3EH
3SF
4.4
50Y
50Z
51W
51X
52M
52N
52O
52P
52S
52T
52U
52W
52X
53G
5GY
5HH
5LA
5VS
66C
702
7PT
8-0
8-1
8-3
8-4
8-5
8UM
930
A03
AAESR
AAEVG
AAHBH
AAHHS
AANLZ
AAONW
AASGY
AAXRX
AAZKR
ABCQN
ABCUV
ABDPE
ABEML
ABJNI
ABPVW
ACAHQ
ACBNA
ACBWZ
ACCFJ
ACCZN
ACFBH
ACGFO
ACGFS
ACGOD
ACIWK
ACKIV
ACPOU
ACPRK
ACSCC
ACXBN
ACXQS
ADBBV
ADEOM
ADIZJ
ADKYN
ADMGS
ADOZA
ADXAS
ADZMN
AEEZP
AEGXH
AEIGN
AEIMD
AENEX
AEQDE
AEUQT
AEUYR
AFBPY
AFFDN
AFFPM
AFGKR
AFPWT
AFRAH
AFZJQ
AHBTC
AHEFC
AI.
AIAGR
AITYG
AIURR
AIWBW
AJBDE
AJXKR
ALAGY
ALMA_UNASSIGNED_HOLDINGS
ALUQN
AMBMR
AMYDB
ATUGU
AUFTA
AZBYB
AZFZN
AZVAB
BAFTC
BDRZF
BFHJK
BHBCM
BKOMP
BMNLL
BMXJE
BNHUX
BROTX
BRXPI
BSCLL
BY8
CAG
COF
CS3
D-E
D-F
D-I
DC6
DCZOG
DPXWK
DR2
DRFUL
DROCM
DRSTM
DU5
EBS
EJD
ESX
F00
F01
F04
F5P
FEDTE
FZ0
G-S
G.N
GODZA
H.T
H.X
HF~
HGLYW
HVGLF
HZ~
IX1
J0M
K48
LATKE
LC2
LC3
LEEKS
LH4
LITHE
LOXES
LP6
LP7
LUTES
LW6
LYRES
MEWTI
MK4
MRFUL
MRSTM
MSFUL
MSSTM
MXFUL
MXSTM
N04
N05
N9A
NEJ
NF~
O66
O9-
OIG
P-O
P2P
P2W
P2X
P4D
PALCI
PQQKQ
Q.N
Q11
QB0
R.K
RIWAO
RJQFR
RNS
ROL
RX1
RXW
SAMSI
SJN
SUPJJ
TAE
TN5
UB1
UBH
UHB
UKR
V8K
VH1
W8V
W99
WBFHL
WBKPD
WH7
WIH
WIK
WOHZO
WQJ
WRC
WXSBR
WYISQ
XG1
XOL
Y6R
YQJ
ZCA
ZCG
ZGI
ZT4
ZXP
ZZTAW
~IA
~KM
~WT
G8K
08R
AAJUZ
ABCVL
ABHUG
ABPTK
ABWRO
ACSMX
ACXME
ADAWD
ADDAD
AFDAS
AFMIJ
AFVGU
AGJLS
IQODW
XFK
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QO
7QR
7ST
7T7
7U7
8FD
C1K
F28
FR3
P64
RC3
SOI
7X8
ID FETCH-LOGICAL-c5293-85fa9eccee7ccb6c86ae22c8e6cbaa4455ff4a41fc18e349baf9b560d319ed363
IEDL.DBID DR2
ISSN 0022-1147
IngestDate Fri Aug 16 22:17:51 EDT 2024
Fri Aug 16 04:49:24 EDT 2024
Fri Aug 16 06:29:22 EDT 2024
Thu Oct 10 16:40:47 EDT 2024
Fri Aug 23 02:15:53 EDT 2024
Sat Sep 28 08:00:40 EDT 2024
Sun Oct 22 16:09:24 EDT 2023
Sat Aug 24 00:54:52 EDT 2024
Wed Oct 30 09:55:08 EDT 2024
IsPeerReviewed true
IsScholarly true
Issue 1
Keywords Validation
Correlation
ricin
biological activity assay
Enzyme immunoassay
Detection
Activation energy
ELISA assay
Biological activity
Immunological method
ELISA
Language English
License CC BY 4.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c5293-85fa9eccee7ccb6c86ae22c8e6cbaa4455ff4a41fc18e349baf9b560d319ed363
Notes ArticleID:JFDS1943
istex:06DF085B749E34AF5E70D38513E2AB281753E91D
ark:/67375/WNG-V0PDW01Q-R
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Article-2
ObjectType-Feature-1
PMID 21535638
PQID 853592167
PQPubID 23500
PageCount 5
ParticipantIDs proquest_miscellaneous_864787525
proquest_miscellaneous_861539375
proquest_miscellaneous_1770340727
proquest_journals_853592167
crossref_primary_10_1111_j_1750_3841_2010_01943_x
pubmed_primary_21535638
pascalfrancis_primary_23843523
wiley_primary_10_1111_j_1750_3841_2010_01943_x_JFDS1943
istex_primary_ark_67375_WNG_V0PDW01Q_R
PublicationCentury 2000
PublicationDate 2011-01
January/February 2011
2011
2011 Jan-Feb
2011-01-00
20110101
PublicationDateYYYYMMDD 2011-01-01
PublicationDate_xml – month: 01
  year: 2011
  text: 2011-01
PublicationDecade 2010
PublicationPlace Malden, USA
PublicationPlace_xml – name: Malden, USA
– name: Hoboken, NJ
– name: United States
– name: Chicago
PublicationTitle Journal of food science
PublicationTitleAlternate J Food Sci
PublicationYear 2011
Publisher Blackwell Publishing Inc
Wiley
Wiley Subscription Services, Inc
Publisher_xml – name: Blackwell Publishing Inc
– name: Wiley
– name: Wiley Subscription Services, Inc
References Olsnes S, Refsnes K, Pihl A. 1974. Mechanism of action of the toxic lectins abrin and ricin. Nature 249:627-31.
Centers for Disease Control and Prevention. 2000. Biological and chemical terrorism: strategic plan for preparedness and response-recommendations of the CDC strategic planning workshop. Morb Mortal Wkly Rep 49:1-14.
Ler SG, Lee FK, Gopalakrishnakone P. 2006. Trends in detection of warfare agents: detection methods for ricin, staphylococcal enterotoxin B and T-2 toxin. J Chromatogr 1133:1-12.
Barbieri L, Valbonesi P, Bonora E, Gorini P, Bolognesi A, Stirpe F. 1997. Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins: effect on DNA, RNA, and poly (A). Nucleic Acids Res 25:518-22.
Labuza TP. 1984. Application of chemical kinetics to deterioration of foods. J Chem Edu 61:348-58.
McCann WP, Hall LM, Siler W, Barton N, Whitley RJ. 1985. High-pressure liquid chromatographic methods for determining arabinosyladenine-5'-monophosphate, arabinosyladenine, and arabinosylhypoxanthine in plasma and urine. Antimicrob Agents Chemother 28:265-73.
Thorn F, Stockhausen H, Germann T, Frosch S, Wade EJ. 2005. Biological inactivation and impaired detection of IL-10 by sumarin. J Immunol Methods 299:91-8.
Zamboni M, Brigotti M, Rambellie F, Montanaro L. 1989. High-pressure-liquid-chromatographic and fluorometric methods for the determination of adenine released from ribosomes by ricin and gelonin. Biochem J 259:639-43.
Griffiths GD, Newman H, Gee DJ. 1986. Identification and quantification of ricin toxin in animal tissues using ELISA. J Forensic Sci Soc 26:349-58.
Kost AA, Ivanov MV. 1980. Etheno derivatives of adenine and cytosine. Chem Heterocycl Compd 3:209-305.
Becher F, Duriez H, Volland JC, Ezan E. 2007. Detection of functional ricin by immunoaffinity and liquid chromatography-tandem mass spectrometry. Anal Chem 79:659-65.
Koja N, Shibata T, Mochida K. 1980. Enzyme-linked immunoassay of ricin. Toxicon 18:611-618.
Brigotti M, Barbieri L, Valbonesi P, Stirpe F, Montanaro L, Sperti S. 1998. A rapid and sensitive method to measure the enzymatic activity of ribosome inactivating proteins. Nucleic Acids Res 26:4306-7.
Endo Y, Tsurugi K. 1987. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J Biol Chem 262:8128-30.
Sturm MB, Schramm VL. 2009. Detecting ricin: sensitive luminescent assay for ricin A-chain ribosome depurination kinetics. Anal Chem 81:2847-53.
Xu S, Labuza TP, Diez-Gonzalez F. 2006. Thermal inactivation of Bacillus anthracis spores in cow's milk. Appl Environ Microbiol 72:4479-83.
Barrio JR, Secrist JA, Leonard NJ. 1972. Fluorescent adenosine and cytidine derivatives. Biochem Biophys Res Commun 46:597-604.
Kochetkov NK, Shibaev VN, Kost AA. 1972. Modification of nucleic acid components with α-haloaldehydes. Dokl Akad Nauk SSSR 205:100-3.
Leith AG, Griffiths GD, Green MA. 1988. Quantification of ricin toxin using a highly sensitive avidin/biotin enzyme-linked immunoassay. J Forensic Sci Soc 28:227-36.
Barbieri L, Valbonesi P, Righi F, Zuccheri G, Monti F, Gorini P, Samori B, Stirpe F. 2000. Polynucleotide:adenosine glycosidase is the sole activity of ribosome-inactivating proteins on DNA. J Biochem 128:883-9.
Kochetkov NK, Shibaev VN, Kost AA. 1971. New reaction of adenine and cytosine derivatives potentially useful for nucleic acids modifications. Tetrahedron Lett 22:1993-6.
Labuza TP. 1979. A theoretical comparison of losses in foods under fluctuating temperature sequences. J Food Sci 44:1162-68.
Jackson LS, Tolleson WH, Chirtel SJ. 2006. Thermal inactivation of ricin using infant formula as food matrix. J Agric Food Chem 54:7300-4.
1987; 262
1984; 61
1998; 26
1971; 22
1985; 28
1989; 259
2000; 49
2006; 72
1980; 18
2009; 81
2006; 54
2005; 299
2000; 128
1997; 25
1986; 26
1980; 3
1988; 28
1974; 249
1983
2006; 1133
1972; 46
1979; 44
2007; 79
1972; 205
Labuza TP (e_1_2_6_16_1) 1983
e_1_2_6_21_1
e_1_2_6_10_1
e_1_2_6_20_1
Centers for Disease Control and Prevention (e_1_2_6_7_1) 2000; 49
e_1_2_6_9_1
e_1_2_6_8_1
e_1_2_6_19_1
e_1_2_6_5_1
Kochetkov NK (e_1_2_6_12_1) 1972; 205
e_1_2_6_4_1
e_1_2_6_6_1
e_1_2_6_13_1
e_1_2_6_25_1
e_1_2_6_14_1
e_1_2_6_24_1
e_1_2_6_3_1
e_1_2_6_11_1
e_1_2_6_23_1
e_1_2_6_2_1
e_1_2_6_22_1
e_1_2_6_17_1
e_1_2_6_18_1
e_1_2_6_15_1
References_xml – volume: 3
  start-page: 209
  year: 1980
  end-page: 305
  article-title: Etheno derivatives of adenine and cytosine
  publication-title: Chem Heterocycl Compd
– volume: 49
  start-page: 1
  year: 2000
  end-page: 14
  article-title: Biological and chemical terrorism: strategic plan for preparedness and response—recommendations of the CDC strategic planning workshop
  publication-title: Morb Mortal Wkly Rep
– start-page: 71
  year: 1983
  end-page: 116
– volume: 26
  start-page: 4306
  year: 1998
  end-page: 7
  article-title: A rapid and sensitive method to measure the enzymatic activity of ribosome inactivating proteins
  publication-title: Nucleic Acids Res
– volume: 54
  start-page: 7300
  year: 2006
  end-page: 4
  article-title: Thermal inactivation of ricin using infant formula as food matrix
  publication-title: J Agric Food Chem
– volume: 18
  start-page: 611
  year: 1980
  end-page: 618
  article-title: Enzyme‐linked immunoassay of ricin
  publication-title: Toxicon
– volume: 26
  start-page: 349
  year: 1986
  end-page: 58
  article-title: Identification and quantification of ricin toxin in animal tissues using ELISA
  publication-title: J Forensic Sci Soc
– volume: 79
  start-page: 659
  year: 2007
  end-page: 65
  article-title: Detection of functional ricin by immunoaffinity and liquid chromatography‐tandem mass spectrometry
  publication-title: Anal Chem
– volume: 128
  start-page: 883
  year: 2000
  end-page: 9
  article-title: Polynucleotide:adenosine glycosidase is the sole activity of ribosome‐inactivating proteins on DNA
  publication-title: J Biochem
– volume: 61
  start-page: 348
  year: 1984
  end-page: 58
  article-title: Application of chemical kinetics to deterioration of foods
  publication-title: J Chem Edu
– volume: 249
  start-page: 627
  year: 1974
  end-page: 31
  article-title: Mechanism of action of the toxic lectins abrin and ricin
  publication-title: Nature
– volume: 25
  start-page: 518
  year: 1997
  end-page: 22
  article-title: Polynucleotide:adenosine glycosidase activity of ribosome‐inactivating proteins: effect on DNA, RNA, and poly (A)
  publication-title: Nucleic Acids Res
– volume: 81
  start-page: 2847
  year: 2009
  end-page: 53
  article-title: Detecting ricin: sensitive luminescent assay for ricin A‐chain ribosome depurination kinetics
  publication-title: Anal Chem
– volume: 259
  start-page: 639
  year: 1989
  end-page: 43
  article-title: High‐pressure‐liquid‐chromatographic and fluorometric methods for the determination of adenine released from ribosomes by ricin and gelonin
  publication-title: Biochem J
– volume: 22
  start-page: 1993
  year: 1971
  end-page: 6
  article-title: New reaction of adenine and cytosine derivatives potentially useful for nucleic acids modifications
  publication-title: Tetrahedron Lett
– volume: 44
  start-page: 1162
  year: 1979
  end-page: 68
  article-title: A theoretical comparison of losses in foods under fluctuating temperature sequences
  publication-title: J Food Sci
– volume: 72
  start-page: 4479
  year: 2006
  end-page: 83
  article-title: Thermal inactivation of spores in cow's milk
  publication-title: Appl Environ Microbiol
– volume: 28
  start-page: 265
  year: 1985
  end-page: 73
  article-title: High‐pressure liquid chromatographic methods for determining arabinosyladenine‐5’‐monophosphate, arabinosyladenine, and arabinosylhypoxanthine in plasma and urine
  publication-title: Antimicrob Agents Chemother
– volume: 299
  start-page: 91
  year: 2005
  end-page: 8
  article-title: Biological inactivation and impaired detection of IL‐10 by sumarin
  publication-title: J Immunol Methods
– volume: 1133
  start-page: 1
  year: 2006
  end-page: 12
  article-title: Trends in detection of warfare agents: detection methods for ricin, enterotoxin B and T‐2 toxin
  publication-title: J Chromatogr
– volume: 46
  start-page: 597
  year: 1972
  end-page: 604
  article-title: Fluorescent adenosine and cytidine derivatives
  publication-title: Biochem Biophys Res Commun
– volume: 262
  start-page: 8128
  year: 1987
  end-page: 30
  article-title: RNA ‐glycosidase activity of ricin A‐chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
  publication-title: J Biol Chem
– volume: 205
  start-page: 100
  year: 1972
  end-page: 3
  article-title: Modification of nucleic acid components with α‐haloaldehydes
  publication-title: Dokl Akad Nauk SSSR
– volume: 28
  start-page: 227
  year: 1988
  end-page: 36
  article-title: Quantification of ricin toxin using a highly sensitive avidin/biotin enzyme‐linked immunoassay
  publication-title: J Forensic Sci Soc
– ident: e_1_2_6_8_1
  doi: 10.1016/S0021-9258(18)47538-2
– ident: e_1_2_6_17_1
  doi: 10.1021/ed061p348
– ident: e_1_2_6_24_1
  doi: 10.1128/AEM.00096-06
– volume: 205
  start-page: 100
  year: 1972
  ident: e_1_2_6_12_1
  article-title: Modification of nucleic acid components with α‐haloaldehydes
  publication-title: Dokl Akad Nauk SSSR
  contributor:
    fullname: Kochetkov NK
– ident: e_1_2_6_23_1
  doi: 10.1016/j.jim.2005.01.008
– ident: e_1_2_6_19_1
  doi: 10.1016/j.chroma.2006.08.078
– ident: e_1_2_6_6_1
  doi: 10.1093/nar/26.18.4306
– ident: e_1_2_6_11_1
  doi: 10.1016/S0040-4039(01)96762-0
– start-page: 71
  volume-title: Chapter 4. Computer‐aided techniques in food technology
  year: 1983
  ident: e_1_2_6_16_1
  contributor:
    fullname: Labuza TP
– ident: e_1_2_6_10_1
  doi: 10.1021/jf061199n
– ident: e_1_2_6_21_1
  doi: 10.1038/249627a0
– ident: e_1_2_6_18_1
  doi: 10.1016/S0015-7368(88)72840-6
– ident: e_1_2_6_2_1
  doi: 10.1093/nar/25.3.518
– ident: e_1_2_6_9_1
  doi: 10.1016/S0015-7368(86)72516-4
– ident: e_1_2_6_14_1
  doi: 10.1007/BF02401711
– ident: e_1_2_6_22_1
  doi: 10.1021/ac8026433
– ident: e_1_2_6_4_1
  doi: 10.1016/S0006-291X(72)80181-5
– ident: e_1_2_6_20_1
  doi: 10.1128/AAC.28.2.265
– ident: e_1_2_6_5_1
  doi: 10.1021/ac061498b
– volume: 49
  start-page: 1
  year: 2000
  ident: e_1_2_6_7_1
  article-title: Biological and chemical terrorism: strategic plan for preparedness and response—recommendations of the CDC strategic planning workshop
  publication-title: Morb Mortal Wkly Rep
  contributor:
    fullname: Centers for Disease Control and Prevention
– ident: e_1_2_6_15_1
  doi: 10.1111/j.1365-2621.1979.tb03472.x
– ident: e_1_2_6_25_1
  doi: 10.1042/bj2590639
– ident: e_1_2_6_3_1
  doi: 10.1093/oxfordjournals.jbchem.a022827
– ident: e_1_2_6_13_1
  doi: 10.1016/0041-0101(80)90088-4
SSID ssj0002236
Score 2.0718486
Snippet :  The suitability of enzyme‐linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally...
The suitability of enzyme-linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally...
The suitability of enzyme‐linked immunosorbent assay (ELISA) for residual ricin toxicity determination was investigated in this study. Ricin was thermally...
SourceID proquest
crossref
pubmed
pascalfrancis
wiley
istex
SourceType Aggregation Database
Index Database
Publisher
StartPage C112
SubjectTerms activation energy
Adenine - metabolism
Assaying
Biological
biological activity assay
Biological and medical sciences
Chemical Warfare Agents - analysis
Chemical Warfare Agents - toxicity
correlation
DNA - metabolism
ELISA
Enzyme-Linked Immunosorbent Assay
Enzymes
Food Contamination
Food industries
Food Inspection - methods
Food science
Foods
Fundamental and applied biological sciences. Psychology
Half-Life
Hot Temperature
Kinetics
Protein Stability
Proteins
ricin
Ricin - analysis
Ricin - toxicity
Toxicity
Toxins
Toxins, Biological - analysis
Toxins, Biological - toxicity
Validation studies
Title Validation of Immunodetection (ELISA) of Ricin Using a Biological Activity Assay
URI https://api.istex.fr/ark:/67375/WNG-V0PDW01Q-R/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1750-3841.2010.01943.x
https://www.ncbi.nlm.nih.gov/pubmed/21535638
https://www.proquest.com/docview/853592167
https://search.proquest.com/docview/1770340727
https://search.proquest.com/docview/861539375
https://search.proquest.com/docview/864787525
Volume 76
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZQOcCF9yMUKiMhBIeskviR5Lhiu7QVVGVLHzfLduzLSlnU7EqFX8-MnWzZqiCEkHKIlHGUjOfxOfk8Q8ibRnDLOWNpZb1JualNaryTKUAjLSHdmizsSvt8KPdO-MG5OO_5T7gXJtaHWH9wQ88I8RodXJtu08kh26Ws4nnP0IL1OBshnsxZieyuyeyqkhRkQTkUDoclQHmN1HPTjTYy1W1U-iUyJ3UHyvOx68VNsHQT5YY0Nb1P5sMLRnbKfLRampH9ca324__RwANyr0ezdBzN7yG55dpH5M6w2bl7TI5OAefHtk104ek-7kZZNG4ZCGAtfbf7af94_B4vzfAXPw0MBqppbJGJBkTHNja4oGBJ-vsTcjLd_fphL-2bOKRWAJRIK-F1DXbiXGmtkbaS2hWFrZy0RmvOhfCea557m1eO8dpoXxuAYQ3EBtcwyZ6SrXbRuueEmhoyqTUsa7zhWjsQ81mNGM5VgnOdkHyYMPUt1upQv6xxQFcKdaVQVyroSl0m5G2Y2fUAfTFHrlsp1NnhR3WaHU3OsvyLmiVkZ2Pq1wMA8wDkLFhCtgdbUH0c6BSAIVEXuSwT8np9FRwY_8ro1i1WHTwXBF0sUwcy9DcyFcJyAJLiTyJYZkkUIPIsGuLVE8JgAXE2IWUwp79WjjqYTo7x9MU_j9wmd-NXeDxekq3lxcq9Ahi3NDvBQX8CJgc3CQ
link.rule.ids 315,783,787,1378,4031,27935,27936,27937,46306,46730
linkProvider Wiley-Blackwell
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3db9MwELfQ9jBeYOMzGxtGQggeUiWxnY_Hal1pR1eN7vPNsh37ZShFaysN_nru4qRbp4EQQspDJJ8j53wfP9vnO0Lel4IbzhkLc-N0yHWhQ-1sGgI0Uim4Wx3Vt9KOxungjB9eisumHBDehfH5IZYbbqgZtb1GBccN6VUtB3cXspzHTYgWLMhZBwDlOmg_wzoOvcltLinwg2mbOhwWAdm9sJ6HvrTiq9aR7TcYO6lmwD7n6148BExXcW7tqPpPybf2F318ylVnMdcd8_Ne9sf_xINN8qQBtLTrJXCLPLLVM7LR3neePSfH5wD1feUmOnV0iBdSpqWd1zFgFf14MBqedD9h0wRP-WkdxEAV9VUyUYZo1_gaFxSESf14Qc76B6f7g7Cp4xAaAWgizIVTBYiKtZkxOjV5qmySmNymRivFuRDOccVjZ-LcMl5o5QoNSKwE82BLlrKXZK2aVvY1oboAZ2o0i0qnuVIWyFxUIIyzueBcBSRuZ0x-9-k65J1lDvBKIq8k8krWvJI3AflQT-2yg7q-wnC3TMiL8Wd5Hh33LqL4q5wEZG9l7pcdAPYA6kxYQHZaYZCNKZhJwEOiSOI0C8i7ZSvoMB7MqMpOFzMYF9hdzFQHNPQ3NDkic8CS4k8kmGlJJEDyykvi7QihswBTG5Cslqe_Zo487PdO8HX7n3u-JRuD06ORHA3HX3bIY78pj88bsja_XthdQHVzvVdr6y-Hpjsh
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3db9MwELfQJgEvfH-EwTASQvCQKh-2kzxWdGUdoyod-3izbMd-qZROaysN_nru7KSj00AIIeUhks-Rc76Pn-3zHSFva84MY3kel8bpmOlKx9pZEQM0UgLcrU78rbQvY7F_zA7O-Fkb_4R3YUJ-iPWGG2qGt9eo4Oe121Ry8HZxXrK0jdCC9XjeAzy5zQQAYQRI06tUUuAGRZc5HNYAxbWonpu-tOGqtpHrlxg6qRbAPRfKXtyESzdhrvdTw_tk1v1hCE-Z9VZL3TM_riV__D8seEDutXCW9oP8PSS3bPOI3OluOy8ek8kJAP1Qt4nOHR3hdZR5bZc-Aqyh7_cOR0f9D9g0xTN-6kMYqKKhRiZKEO2bUOGCgiip70_I8XDv28f9uK3iEBsOWCIuuVMVCIq1hTFamFIom2WmtMJopRjj3DmmWOpMWtqcVVq5SgMOq8E42DoX-VOy1cwb-5xQXYErNTpPaqeZUhbIXFIhiLMlZ0xFJO0mTJ6HZB3yl0UO8EoiryTySnpeycuIvPMzu-6gLmYY7FZweTr-JE-SyeA0Sb_KaUR2N6Z-3QFAD2DOLI_ITicLsjUECwloiFdZKoqIvFm3ggbjsYxq7Hy1gHGB1cU8dUBDf0NTIi4HJMn_RIJ5lngGJM-CIF6NEDpzMLQRKbw4_TVz5MFwcISvL_6552tyezIYysPR-PMOuRt25PF5SbaWFyv7CiDdUu96Xf0JkbA50A
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=Validation+of+Immunodetection+%28ELISA%29+of+Ricin+Using+a+Biological+Activity+Assay&rft.jtitle=Journal+of+food+science&rft.au=LUMOR%2C+Stephen+E&rft.au=HUTT%2C+Aaron&rft.au=RONNINGEN%2C+Ian&rft.au=DIEZ-GONZALEZ%2C+Francisco&rft.date=2011&rft.pub=Wiley&rft.issn=0022-1147&rft.eissn=1750-3841&rft.volume=76&rft.issue=1&rft_id=info:doi/10.1111%2Fj.1750-3841.2010.01943.x&rft.externalDBID=n%2Fa&rft.externalDocID=23843523
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-1147&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-1147&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-1147&client=summon