Subcellular localization of branched-chain amino acid aminotransferase and lactate dehydrogenase C4 in rat and mouse spermatozoa.
Spermatozoa isolated from rat and mouse epididymes show a relatively high branched-chain amino acid aminotransferase (leucine aminotransferase, EC 2.6.1.6) activity. There is a significant reduction of leucine aminotransferase and of the isoenzyme C4 of lactate dehydrogenase (EC 1.1.1.27) in the gametes during their epididymal transit. Studies of patterns of liberation of the leucine aminotransferase and of the lactate dehydrogenase C4 from intact spermatozoa, treated with increasing concentrations of digitonin, indicate that both enzymes have the same dual subcellular location, i.e. in the cytosol and in the mitochondria.
Montamat
E E
EE
Cátedra de Química Biológica, Facultad de Ciencias Médicas, Universidad Nacional de Córdoba, Argentina.
Vermouth
N T
NT
Blanco
A
A
D000818:Animals; D004072:Digitonin / Q000494:pharmacology; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D051276:Leucine Transaminase; D008297:Male; D051379:Mice; D051381:Rats; D011919:Rats, Inbred Strains; D013094:Spermatozoa / Q000187:drug effects / Q000201:enzymology*; D013347:Subcellular Fractions / Q000187:drug effects / Q000201:enzymology; D013737:Testis / Q000201:enzymology; D000637:Transaminases / Q000378:metabolism*
D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D000637:Transaminases; D051276:Leucine Transaminase; D004072:Digitonin