Human serum carnosinase: characterization, distinction from cellular carnosinase, and activation by cadmium

Abstract

Human serum carnosinase was assayed using a simple and sensitive fluorometric method. Under optimum conditions, the average adult serum hydrolyzed 42 mu mol of carnosine per ml per hour, about 17 times the average activity reported in the literature. Cadmium was twice as effective as manganese as an activator of this enzyme. Serum carnosinase was found to be different in many respects from cellular carnosinase. For example, the serum isozyme hydrolyzed homocarnosine, whereas the cellular carnosinase did not. The apparent molecular weight of serum carnosinase was 160 000, while that of the cellular isozyme was 90 000. Although it has been reported that serum contains two molecular forms of carnosinase, only one form was detected using several electrophoretic methods and two ion exchange chromatography procedures. The concentration of serum carnosinase varied greatly between individuals. Little or no enzyme was detected in children below 10 months in age. Thereafter, the average concentration of carnosinase increased gradually to reach the adult range at age 13-15.