[Activity and molecular forms of nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-dependent malate dehydrogenase in bull spermatozoa].
Investigations were carried out on the activity and the isoenzyme composition of the NAD- and NADP-dependent malatedehydrogenase in the soluble and sedimental proteins of bull spermatozoa. It was found that the activity of the NAD-dependent malatedehydrogenase was higher than the activity of the NADP-dependent one both in the soluble and in the sedimental proteins. The difference in the activity was spectrophotometrically and electrophoretically demonstrated.
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000032:analysis*; D008291:Malate Dehydrogenase / Q000032:analysis*; D008297:Male; D009243:NAD; D009249:NADP; D011506:Proteins / Q000032:analysis; D012995:Solubility; D013053:Spectrophotometry; D013094:Spermatozoa / Q000032:analysis / Q000201:enzymology*
D007527:Isoenzymes; D011506:Proteins; D009243:NAD; D009249:NADP; D008291:Malate Dehydrogenase; C031917:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Avtivnost i molekuliarni formi na nikotinamidadenindinukleotid- i nikotinamidadenindinukleotidfosfat-zavisimata malatdekhidrogenaza v spermatozoidi na bik.