Abstract
Summary
The extraction of rabbit spermatozoa with the MgCl2 treatment, followed by chromatography of extracts on a DEAE-cellulose column, yield highly purified aryl sulfatases. The enzyme preparation showed one major band with the possibility of a minor contaminant by acrylamide gel electrophoresis. The single band had two activities, that of aryl sulfatases A and B. Aryl sulfatase C was not detectable. The purified aryl sulfatases had optima at pH's 4.8, 5.6, and 6.0. The enzymes exhibited no activity at 4° but exhibited. higher activity at 50° than at 37°. The pure aryl sulfatases had higher affinity for p-nitrocatechol sulfate than for p-nitrophenol sulfate. Phosphate and sulfite ions inhibited the enzymes, but NaCl, KCl, and sulfate did not. Rabbit, ram, bull, and boar sperm acrosomal extracts showed high aryl sulfatase activities.
The authors thank Mrs. Diane Fitzgerald for her skillful technical assistance.
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