Determination of Aflatoxin B1–DNA Adduct in Rat Liver by Enzyme Immunoassay

The Analyst ◽  
1997 ◽  
Vol 122 (6) ◽  
pp. 609-613 ◽  
Author(s):  
T. Vidyasagar ◽  
N. Sujatha ◽  
R. B. Sashidhar
1978 ◽  
Vol 75 (4) ◽  
pp. 1745-1749 ◽  
Author(s):  
R. G. Croy ◽  
J. M. Essigmann ◽  
V. N. Reinhold ◽  
G. N. Wogan
Keyword(s):  

2011 ◽  
Vol 41 (7) ◽  
pp. 1177-1183 ◽  
Author(s):  
Hui CHEN ◽  
Jin-Ming LIN ◽  
XiTang YING ◽  
GuoMao HU ◽  
GuoJin ZHENG

1995 ◽  
Vol 312 (2) ◽  
pp. 535-541 ◽  
Author(s):  
E M Ellis ◽  
J D Hayes

The enzyme from rat liver that reduces aflatoxin B1-dialdehyde exhibits a unique catalytic specificity distinct from that of other aldo-keto reductases. This enzyme, designated AFAR, displays high activity towards dicarbonyl-containing compounds with ketone groups on adjacent carbon atoms; 9,10-phenanthrenequinone, acenaphthenequinone and camphorquinone were found to be good substrates. Although AFAR can also reduce aromatic and aliphatic aldehydes such as succinic semialdehyde, it is inactive with glucose, galactose and xylose. The enzyme also exhibits low activity towards alpha, beta-unsaturated carbonyl-containing compounds. Determination of the apparent Km reveals that AFAR has highest affinity for 9,10-phenanthrenequinone and succinic semialdehyde, and low affinity for glyoxal and DL-glyceraldehyde.


1996 ◽  
Vol 30 (1) ◽  
pp. 138-144
Author(s):  
D. GAYLE DEBORD ◽  
KENNETH L. CHEEVER ◽  
DWIGHT M. WERREN ◽  
THOMAS M. REID ◽  
TERRI F. SWEARENGIN ◽  
...  

Talanta ◽  
2013 ◽  
Vol 107 ◽  
pp. 25-29 ◽  
Author(s):  
Feng-Yih Yu ◽  
Anastasia V. Gribas ◽  
Marina M. Vdovenko ◽  
Ivan Yu. Sakharov

1992 ◽  
Vol 13 (6) ◽  
pp. 1031-1033 ◽  
Author(s):  
Audrey Zarba ◽  
Robert Himieleski ◽  
David R. Hemenway ◽  
George J. Jakab ◽  
John D. Groopman

2021 ◽  
Vol 80 (Suppl 1) ◽  
pp. 1083.2-1084
Author(s):  
O. Rusanova ◽  
A. Trofimenko ◽  
N. Emelyanov ◽  
O. Emelyanova

Background:Production of antibodies to ceruloplasmin (CP) in rheumatoid arthritis is an issue that has not been studied well enough. It was not by chance that this copper–containing alpha 2-glycorpoteid of blood plasma showing multienzymatic properties was chosen as an object of investigation. Data on the content and activity of CP in the blood of rheumatoid arthritis patients are contradictory, which has to do with different approaches to selection of patients and different measuring methods.Objectives:Improving diagnosis of rheumatoid arthritis by determination of antibodies to CP as well as its amount and enzymatic activity.Methods:We studied the serum from 30 apparently healthy individuals, and 108 rheumatoid arthritis patients. Antibodies to CP were determined by enzyme immunoassay using immobilized granulated antigen preparations (modification by Gontar et al, 2002). The amount of CP was determined by enzyme immunoassay according to the method of I.S. Kuzmina et al (1991) using commercial diagnostic agent manufactured by Mechnikov Research Institute for Vaccines and Sera.Results:Enzyme immunoassay showed a mean level of CP antibodies in donor sera of 0,020±0,006 optical density units. The level of normal values of specific antibodies determined as M±2σ included an extinction value in the range 0 – 0,086. The mean value of oxidase activity and the amount of CP in healthy people was 716±26,3 and 921±32 ng/ml, correspondingly. In the process of study we revealed a reliable increase in CP antibody count, the activity and amount of CP in patients with rheumatoid arthritis while in all cases the parameters under study correlated with the degree of disease activity (p<0,05): at activity degree I CP antibodies were 0,098±0,011; CP activity was 954±48,1; CP amount was 1292±73,4. At activity degree II CP antibodies were 0,138±0,007; CP activity was 1163±39,6; CP amount was 1763±69,3. At activity degree III, CP antibodies were 0,182±0,015; CP activity was 1368±89,5; CP amount was 1794±102,8. After a course of hospital treatment was completed, we noted a reliable decrease in the activity and amount of CP (at degree I of rheumatoid arthritis activity p<0,001, at degree II of rheumatoid arthritis activity p<0,01for both parameters; at degree III, p<0,05) compared with baseline findings. A decrease in CP antibodies shows decelerated dynamics, especially in patients with pronounced disease activity, which indicates severe disorders in the immunity that cannot be cured completely within 30 – 40 days of hospital treatment course.Conclusion:Determination of CP antibodies, as well as quantitative content of CP and its oxidase activity can serve as indicators of the activity of rheumatoid arthritis, as well as an accessory criterion of the effectiveness of administered therapy.Disclosure of Interests:None declared


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