Species identification of ancient leather objects by the use of the enzyme-linked immunosorbent assay

2016 ◽  
Vol 8 (42) ◽  
pp. 7689-7695 ◽  
Author(s):  
Yi Liu ◽  
Yi Li ◽  
Runxing Chang ◽  
Hailing Zheng ◽  
Yang Zhou ◽  
...  
Keyword(s):  
Species Identification ◽  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Immunological Method

A novel immunological method for the species identification of ancient leather.

Assessment of Two Enzyme-Linked Immunosorbent Assay Tests Marketed for Detection of Ruminant Proteins in Finished Feed

2007 ◽  
Vol 70 (3) ◽  
pp. 692-699 ◽  
Author(s):  
MICHAEL J. MYERS ◽  
HAILE F. YANCY ◽  
DOROTHY E. FARRELL ◽  
JEWELL D. WASHINGTON ◽  
CHRISTINE M. DEAVER ◽  
...  
Keyword(s):  
Species Identification ◽  
Immunosorbent Assay ◽  
Correct Response ◽  
Animal Feed ◽  
Elisa Test ◽  
Enzyme Linked Immunosorbent Assay ◽  
Acceptance Criteria ◽  
Sensitivity Assessment ◽  
Identification Test ◽  
The U.S

The performance characteristics of two enzyme-linked immunosorbent assay (ELISA) test kits, ELISA Technologies' MELISA-Tek test and Tepnel BioSystems' BioKit for (Cooked) Species Identification test, designed to detect ruminant proteins in animal feed, were evaluated. The test kits were evaluated by using acceptance criteria developed by the U.S. Food and Drug Administration's Center for Veterinary Medicine Office of Research for evaluating selectivity, sensitivity, ruggedness, and specificity. The acceptance criteria for determining success used a statistical approach requiring a 90% probability of achieving the correct response within a 95% confidence interval. In practice, this measure requires the test to achieve the correct response 58 times for every 60 samples evaluated, or a 96.7% accuracy rate. A minimum detection level of 0.1% bovine meat and bone meal (BMBM) was required, consistent with the sensitivity of the analytical methods presently used by the U.S. Food and Drug Administration. Selectivity was assessed by testing 60 dairy feed samples that contained no added animal proteins; sensitivity was determined by evaluating 60 samples (per level of fortification) of this same feed that contained 0.025, 0.05, 0.1, 0.25, 0.5, 1, or 2% BMBM. The MELISA-Tek test passed the acceptance set-point criteria for selectivity assessment but failed the sensitivity assessment at all levels except at the 2% level. The MELISA-Tek test came close to passing at the 1% level, detecting true-positive findings at a rate of 93%, but failed at lower levels, in spite of the label claim of 0.5% sensitivity. The BioKit for (Cooked) Species Identification test detected only 2 of 17 samples fortified at the 2% BMBM level and failed to detect any other BMBM-fortified samples. The results of this evaluation indicate that neither test is adequate for regulatory use.

scholarly journals Production and Characterization of Monoclonal Antibodies against Vegetative Cells of Bacillus cereus

2000 ◽  
Vol 66 (5) ◽  
pp. 2278-2281 ◽  
Author(s):  
Nadine Charni ◽  
Claude Perissol ◽  
Jean Le Petit ◽  
Nathalie Rugani
Keyword(s):  
Monoclonal Antibodies ◽  
Bacillus Cereus ◽  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Vegetative Cells ◽  
Immunological Method ◽  
Molecular Masses

ABSTRACT Two monoclonal antibodies (MAbs) against Bacillus cereus were produced. The MAbs (8D3 and 9B7) were selected by enzyme-linked immunosorbent assay for their reactivity with B. cereus vegetative cells. They reacted with B. cereusvegetative cells while failing to recognize B. cereusspores. Immunoblotting revealed that MAb 8D3 recognized a 22-kDa antigen, while MAb 9B7 recognized two antigens with molecular masses of approximately 58 and 62 kDa. The use of MAbs 8D3 and 9B7 in combination to develop an immunological method for the detection of B. cereus vegetative cells in foods was investigated.

Development of an immunological method for studying the incorporation of ripening enzymes in cheese curd

1996 ◽  
Vol 63 (1) ◽  
pp. 141-149 ◽  
Author(s):  
Edith Laloy ◽  
Jean-Christophe Vuillemard ◽  
Mouhsine El Abboudi ◽  
Ismael Fliss ◽  
Eric De Grace ◽  
...  
Keyword(s):  
Detection Limit ◽  
Immunosorbent Assay ◽  
Total Protein ◽  
Lactobacillus Casei ◽  
Polyclonal Antibodies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein G ◽  
Immunological Method ◽  
Liposome Suspension ◽  
Cheese Curd

SummaryPolyclonal antibodies raised against partly purified aminopeptidase were specific to cell-free extracts ofLactobacillus caseisubsp.pseudoplantarumUL 137, and did not cross react with any other proteins in Cheddar cheese, at least during the first week of maturation. A sandwich enzyme-linked immunosorbent assay (ELISA) was developed in order to quantify cell-free extracts in the cheese curd, and was also used to determine the efficiency of encapsulation of cell-free extracts in liposomes. This method was very sensitive and exhibited a detection limit of ∼10 μg total protein/g cheese and ∼1 μg total protein/ml liposome suspension. The efficiency of encapsulation of cell-free extracts into liposomes was ∼55–60%. The retention of liposome-encapsulated cell-free extracts was ∼14 times that of non-encapsulated extracts.

Plasminogen Interactions with Immobilized Fibrinogen

1989 ◽  
Vol 62 (04) ◽  
pp. 1078-1082 ◽  
Author(s):  
Burt Adelman ◽  
Patricia Ouynn
Keyword(s):  
Immunosorbent Assay ◽  
Aminocaproic Acid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Binding Regions ◽  
Dose Dependent Fashion ◽  
Epsilon Aminocaproic Acid ◽  
Dose Dependent

SummaryThis report describes the binding of plasminogen to fibrinogen adsorbed onto polystyrene wells. Binding was determined by enzyme linked immunosorbent assay. Both glu- and lys-plasminogen bound to immobilized fibrinogen in a dose-dependent fashion. However, more lys- than glu-plasminogen bound when equal concentrations of either were added to immobilized fibrinogen. Plasminogen binding was inhibited by epsilon aminocaproic acid indicating that binding was mediated via lysine-binding regions of plasminogen. Soluble fibrinogen added in excess of immobilized fibrinogen did not compete for plasminogen binding but fibrinogen fragments produced by plasmin digestion of fibrinogen did. Treatment of immobilized fibrinogen with thrombin caused a small but significant (p <0.01) increase in plasminogen binding. These studies demonstrate that immobilized fibrinogen binds both glu- and lys-plasminogen and that binding is mediated via lysine-binding regions. These interactions may facilitate plasminogen binding to fibrinogen adsorbed on to surfaces and to cells such as platelets which bind fibrinogen.

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