scholarly journals Assessment of Protein G in Serodiagnosis of Zoo Animals and Development of an Enzyme-Linked Immunosorbent Assay for Asian Elephant

2008 ◽  
Vol 61 (1) ◽  
pp. 75-78
Author(s):  
Kentaro SHIMOSAWA ◽  
Naoaki MISAWA
1990 ◽  
Vol 28 (5) ◽  
pp. 913-921 ◽  
Author(s):  
M Harboe ◽  
H G Wiker ◽  
J R Duncan ◽  
M M Garcia ◽  
T W Dukes ◽  
...  

1998 ◽  
Vol 10 (4) ◽  
pp. 326-330 ◽  
Author(s):  
Maurice Lambert ◽  
Michel Calamel ◽  
Philippe Dufour ◽  
Evelyne Cabasse ◽  
Christian Vitu ◽  
...  

In serology, lack of specificity can generally be attributed to cross-reactions between different pathogens with antigens bearing similar epitopes. During seroepidemiologic surveys of contagious agalactia of sheep caused by Mycoplasma agalactiae infection, numerous sera were analyzed by enzyme-linked immunosorbent assay (ELISA). A few sera reacted with various antigens coated on plates, including the well with no antigen. This reactivity was not due to cross-reactions as initially suspected, and these multipositive sera were designated false-positive sera. Elimination of this false positivity was not possible by using covalent ELISA plates or different rabbit anti-sheep IgG conjugates. Only conjugates using monoclonal antibodies or protein G were efficient in elimination of false positivities without reducing the true specific positive titers. No false-positive sera have been observed since the implementation of protein G conjugates in the serologic diagnosis of contagious agalactia by ELISA for the past 2 years.


1998 ◽  
Vol 143 (14) ◽  
pp. 390-394 ◽  
Author(s):  
C. M. Marin ◽  
B. Alonso-Urmeneta ◽  
I. Moriyon ◽  
S. Perez-Gomez ◽  
J. M. Blasco

1996 ◽  
Vol 63 (1) ◽  
pp. 141-149 ◽  
Author(s):  
Edith Laloy ◽  
Jean-Christophe Vuillemard ◽  
Mouhsine El Abboudi ◽  
Ismael Fliss ◽  
Eric De Grace ◽  
...  

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.


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