2003 Volume 51 Issue 3 Pages 361-362
Hepatic cysteinesulfinate aminotransferase activity was studied in fish. Fish liver homogenates were incubated with a reaction mixture containing cysteinesulfinate, 2-oxoglutarate, PLP, NADH, and lactate dehydrogenase for 15 min at 25°C. NADH oxidation was monitored at 340 nm and defined as the enzyme activity. The highest enzyme activity was observed in yellowtail followed by that in red seabream. The lowest level of activity was observed in bluegill. However, the enzyme activities were distributed over a narrow range from 115-430 nmol/min/mg protein. These observations suggest that transamination is a common pathway for cysteinesulfinate metabolism in fish.
