Abstract
Summary
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.
In both preparations, 1 mM N-acetyl-glucosaminolactone completely inhibited staining.
Incubation of bull epididymal preparation with neuraminidase resulted in the disappearance of some of the fast-moving bands and the concomitant deeper staining of the slowmoving bands. Some changes in relative mobility were also observed.
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