Kinetics of the inhibition of aspartate aminotransferase isozymes by DL-glyceraldehyde 3-phosphate.
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In embryos of loach (Misgurnus fossilis) obtained from zygotes, which were incubated for 30 min in the D,L-aspartate solution the alanine aminotransferase activity is 2-4 times as high as in the control embryos. The most essential influence of this amino acid is found in the gastrula -- from 12 till 18 h after fertilization. The aspartate aminotransferase activity under these conditions does not undergo the essential changes. D,L-alanine and adenine do not affect the activity of the both enzymes during primary stages of development, but adenine as well as cytidine reduce the action of aspartate carbamoyltransferase of embryos 3, 6 and 3 h after the beginning of fertilizatio, respectively. The decrease in the aspartate carbamoyltransferase activity is revealed in the unfertilized eggs after 2 h of incubation in the solutions of estrone and thyroxine. Cytidine alone under these conditions has no definite influence, but removes the inhibitory effect of estrone. The regularities were established in changes of the activity of above mentioned enzymes of embryos under physiological conditions of development.
Semen from Manchega and Merina breed rams was subjected to minimal and maximal sperm cell damage treatments. Seminal plasma samples were then analyzed for aspartate aminotransferase (AAT) activity. There were significant (P < 0.01) increases in enzymatic activity after maximal damage treatment in both breeds. Mean values of AAT activity were different between months (P < 0.01) and individual rams (P < 0.01). Breed significantly (P < 0.01) affected AAT activity after minimal and maximal sperm damage. There was an interaction (P < 0.01) between the 2 factors of ram and month in both breeds, but there was no interaction between breed and treatment.