Electrophoresis of NADH-dependent oxidoreductase (diaphorase) in boar spermatozoa.
Two forms of NADH-dependent oxidoreductase (diaphorase [EC.1.6.99.-]) are established in boar spermatozoa. The first form is typical for soluble proteins with a varying electrophoretic profile, while the other form for sedimental proteins with a specific, slowly-moving fraction, which is not common for the soluble form. The two enzyme forms have a close isoelectric point (pI5.5-6.0) and they can not be inhibited by dicumarol 10(-5) mol l-1 and FAD 10(-4) mol l-1. The molecular mass of the soluble form of the enzyme is 28, 37, 46 and 67 kD, while of the sedimental form it is 220, 250 and 260 kD, respectively.
Atanassov
B
B
Institute of Biology and Immunology of Reproduction and Development of Organisms, Bulgarian Academy of Science, Sofia.
Georgiev
G H
GH
D000818:Animals; D008058:Dihydrolipoamide Dehydrogenase / Q000032:analysis* / Q000737:chemistry; D004586:Electrophoresis; D007525:Isoelectric Focusing; D008297:Male; D013094:Spermatozoa / Q000737:chemistry*; D013552:Swine
D008058:Dihydrolipoamide Dehydrogenase