Properties of Arginine Kinase from Drosophila melanogaster

Abstract

1. Starch‐gel electrophoresis of extracts of several strains of the genus Drosophila reveals neither allelic variants nor isoenzymes of arginine kinase. Arginine kinase of the drosophilid Zaprionus vittiger migrates differently. 2. Arginine kinase is non‐uniformly distributed in tissues of Drosophila melanogaster. The activity in muscle tissue represents about 70% of the total activity. A characteristic fluctuation of the enzyme activity during the development from the egg to the adult stage can be observed. 3. Purification of arginine kinase of Drosophila melanogaster has been achieved. Several physico‐chemical properties of the enzyme have been determined. The molecular weight in the range of 40 000 is comparable to other arthropod arginine kinases and suggests that the active enzyme is a monomer. Copyright © 1973, Wiley Blackwell. All rights reserved