scholarly journals Characterization of the binding of the Finland trityl radical with bovine serum albumin

RSC Advances ◽  
2014 ◽  
Vol 4 (88) ◽  
pp. 47649-47656 ◽  
Author(s):  
Yuguang Song ◽  
Yangping Liu ◽  
Wenbo Liu ◽  
Frederick A. Villamena ◽  
Jay L. Zweier

The Finland trityl radical CT-03 binds to bovine serum albumin, inducing the broadening of its EPR signal.

2019 ◽  
Vol 55 (3) ◽  
pp. 318-325
Author(s):  
Xiaofang Wang ◽  
Luyi Zou ◽  
Chenyu Mi ◽  
Hongyan Yu ◽  
Mengxue Dong ◽  
...  

2019 ◽  
Vol 278 ◽  
pp. 203-207 ◽  
Author(s):  
Bo-Bae Koh ◽  
Eun-Jung Lee ◽  
Karna Ramachandraiah ◽  
Geun-Pyo Hong

1986 ◽  
Vol 49 (4) ◽  
pp. 267-271 ◽  
Author(s):  
RU-DONG WEI ◽  
WILLIAM BISCHOFF ◽  
FUN SUN CHU

Antibody raised against T-2 toxin cross-reacted poorly with 3′-OH-T-2 toxin. A new immunogen was prepared by conjugation of hemisuccinate (HS) of 3′-OH-T-2 toxin to bovine serum albumin (BSA). Antibodies against 3′-OH-T-2 toxin were demonstrated by a radioimmunoassay 10 wk after immunization of rabbits with this new immunogen using tritiated 3′-OH-T-2 toxin as the testing ligand. Highest titers (1:6,000) were obtained 17 wk after immunization and two booster injections. The antibodies had good cross-reactivity with T-2 toxin, acetyl-T-2 toxin and 3′-OH-acetyl-T-2 toxin. The relative cross-reactivity of this antibody with 3′-OH-T-2, acetyl-T-2, T-2, 3′-OHacetyl-T-2, 3′-OH-T-2-HS, T-2 isomer, HT-2 and 3′-OH-HT-2 was 1, 3, 4, 5, 15, 30, 45 and 175, respectively. No crossreaction was found when 3′-OH-T-2 triol, T-2-triol, T-2-tetraol, DAS and DON at a concentration of 1 μg per assay was tested. The detection limit for 3′-OH-T-2 toxin by the RIA was about 0.1 ng per assay.


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