Aspartate- and alanine-aminotransferase in early development of keta

We studied the activities of the marker enzymes of physiological state and adaptive reactions, aspartate and alanine aminotransferases, in early development of the keta Oncorhynchus keta. Aspartate aminotransferase with pH optima 6.8, 7.0, 7.6, and 8.0 and alanine aminotransferase with pH optima 7.0, 7.4, 7.6, 7.8, 8.0, and 8.2 were found in the eggs, larvae, and fry. The succession of enzymes with different pH takes place during ontogenesis, as well as stage specific changes in their activity. The maximum enzymatic activity was recorded in the larvae during their rise for "afloat." A correlation was established between the dynamics of enzymatic activity and soluble nitrogen and amine nitrogen contents.     

Aspartate and Alanine Aminotransferases in Early Development of the Keta

We studied the activities of the marker enzymes of physiological state and adaptive reactions, aspartate and alanine aminotransferases, in early development of the keta Oncorhynchus keta. Aspartate aminotransferase with pH optima 6.8, 7.0, 7.6, and 8.0 and alanine aminotransferase with pH optima 7.0, 7.4, 7.6, 7.8, 8.0, and 8.2 were found in the eggs, larvae, and fry. The succession of enzymes with different pH takes place during ontogenesis, as well as stage specific changes in their activity. The maximum enzymatic activity was recorded in the larvae during their rise for afloat. A correlation was established between the dynamics of enzymatic activity and soluble nitrogen and amine nitrogen contents.