Characterization of NAD(P)H diaphorase from boar spermatozoa using specific monoclonal antibodies.
1. After immunization of BALB/c mouse, four monoclonal antibodies against soluble NADH diaphorase from ejaculated boar spermatozoa were produced and characterized. The monoclonal antibodies were designated as follows Mab 1F2, Mab 4E2, Mab 5B8, Mab 5D8. 2. These monoclonal antibodies react with other enzyme forms-sedimentary NADH and NADPH and soluble NADPH and inhibit (although not completely) their activity. It is supposed that different forms of the enzyme share some common epitopes. 3. Treatment of ejaculated boar semen with 2O-methylcholanthrene causes an increase of the activity of the soluble diaphorase form only. 4. These results lead to the assumption that the sperm diaphorase is a dynamic enzyme system consisting of four immunologically similar isoenzymes although their functions are different.
Department of Biochemistry, Bulgarian Academy of Sciences, Sofia.
B
B
Atanassov
S
S
Kyurkchiev
G
G
Georgiev
I
I
Kehayov
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D007114:Immunization; D008297:Male; D008748:Methylcholanthrene; D051379:Mice; D008807:Mice, Inbred BALB C; D009252:NADPH Dehydrogenase / Q000276:immunology / Q000378:metabolism*; D013094:Spermatozoa / Q000201:enzymology*; D013552:Swine
D000911:Antibodies, Monoclonal; D000939:Epitopes; D008748:Methylcholanthrene; D009252:NADPH Dehydrogenase