Microheterogeneity of N-Acetyl- -D-hexosaminidase of Bull Epididymis

Abstract

Most (90%) of the total activity of N-acetyl-β-D-hexosaminidase (EC 3.2.1.30) of bull epididymis homogenate was found in the soluble fraction. Electrophoresis of the soluble fraction on polyacrylamide gel (5.3%) at pH 9.5 separated the enzyme into as many as 12 enzymatically active bands. The bands were successfully stained on the gel using naphthol AS-BI N-acetyl-β-D-glucosaminide as substrate; freed naphthol being coupled with fast garnet GBC. Under similar conditions, human aortic N-acetyl-β-D-hexosaminidase was separated into two bands, namely the A and B forms.