Purification and some properties of human heart arginase.

ABSTRACT

Arginase from extracts of human heart was purified about 1500-fold. In polyacrylamide-gel electrophoresis the enzyme migrated to the cathode at pH 5.5, showing very low mobility at pH 8.9. Molecular weight determined by gel filtration was 120 000. The Km for L-arginine was 5 mM. L-Ornithine and L-lysine were competitive inhibitors. The enzyme was completely inactivated by treatment with EDTA, and dissociated into subunits with mol.wt. of about 30 000. Addition of Mn2+ ions to the inactive subunits resulted in reappearance of the enzyme activity; the molecular weight of the reactivated enzyme corresponded to that of the native form.