A new monoclonal antibody for the sensitive detection of atrazine with immunoassay in microtiter plate and dipstick format

1993 ◽  
Vol 41 (6) ◽  
pp. 1006-1011 ◽  
Author(s):  
Thomas. Giersch
2000 ◽  
Vol 12 (4) ◽  
pp. 253-262 ◽  
Author(s):  
Leif Bruun ◽  
Claus Koch ◽  
Mogens Havsteen Jakobsen ◽  
Jens Aamand

PLoS ONE ◽  
2020 ◽  
Vol 15 (4) ◽  
pp. e0229196
Author(s):  
Shogo Miyoshi ◽  
Soh Tokunaga ◽  
Tatsuhiko Ozawa ◽  
Hiroyuki Takeda ◽  
Mitsuo Aono ◽  
...  

2015 ◽  
Vol 27 (1) ◽  
pp. 111-127 ◽  
Author(s):  
Gabriel Wafula Khaemba ◽  
Bitange Nipa Tochi ◽  
Daniel Mukunzi ◽  
Isanga Joel ◽  
Lingling Guo ◽  
...  

1997 ◽  
Vol 60 (1) ◽  
pp. 64-66 ◽  
Author(s):  
G. ANGUITA ◽  
R. MARTÍN ◽  
T. GARCÍA ◽  
P. MORALES ◽  
A. I. HAZA ◽  
...  

A competitive ELISA (enzyme-linked immunosorbent assay) was performed to detect and quantify bovine milk in ovine and caprine milk and cheese using a monoclonal antibody (AH4 MAb) against bovine β-casein. Ovine or caprine milk and cheese containing bovine milk were added simultaneously with the AH4 MAb to the wells of a microtiter plate that had been previously sensitized with commercial bovine β-casein. The bovine caseins in milk or cheese samples compete with the bovine β-casein bound to the plate for the AH4 MAb binding sites. Further immunorecognition of AH4 MAb bound to the bovine β-casein immobilized onto the plate was attained with rabbit anti-mouse immunoglobulin conjugated to peroxidase. Subsequent enzymic conversion of the substrate showed clear differences in absorbance values during assay of mixtures of ovine and caprine milk and cheese containing various amounts of bovine milk. The competitive ELISA developed in this work allows the quantitative detection of bovine milk in ovine and caprine milk and cheese samples in the range of 0.5 to 25% of substitution.


Author(s):  
Johan Bjerner ◽  
Kari Hauge Olsen ◽  
Ole P. Børmer ◽  
Kjell Nustad

AbstractWe analyzed 95 sera, demonstrating interference in a previous study, with the Kryptor homogeneous time-resolved fluorescence resonance energy transfer carcinoembryonic antigen (CEA) immunoassay (Brahms AG, Berlin, Germany). Only one serum differed, i.e., 6.0 μg/l for Kryptor vs. 13.3 μg/l for a microtiter plate in-house immunofluorometric assay (IFMA), using both aggregated mouse immunoglobulins as blocker and capture monoclonal antibody (Mab) F(ab′)Kryptor-CEA assay results thus agreed with our inhouse CEA assay results, showing no interference. As the Kryptor-CEA assay antibodies were sensitive to interference and the Kryptor-CEA assay buffer did not reduce interference as efficiently as our in-house assay buffer, the Kryptor-CEA assay format was crucial for the absence of interference.


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