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Biology of Reproduction, Vol 12, 232-238, Copyright © 1975 by Society for the Study of Reproduction

Purification of Rabbit Testis Proacrosin and Studies of Its Active Form

Y. H. JOY HUANG-YANG 1, and STANLEY MEIZEL 1

1 Department of Human Anatomy, School of Medicine, University of California, Davis, California 95616 U.S.A.


An inactive form of rabbit testis trypsin-like enzyme appears to be a zymogen. Partial purification of the zymogen is described in detail and includes extraction. Sephadex G-75 gel filtration and SE-Sephadex ion exchange column chromatography at acid pH. The zymogen was separated from a trypsin inhibitor by the Sephadex G-75 chromotographic step, but it still remained inactive unless activated with bovine pancreatic trypsin or "autoactivated" at pH 8. No enzymatic activity could be detected at pH 8 with BAEE as substrate when the zymogen was assayed immediately after pre-incubation at pH 3.

The apparent molecular weights of the zymogen and the trypsin inhibitor as determined by Sephadex G-100 column chromatography were 68,500 ± 2500 and 10,000 respectively.

The activity, produced by autoactivation of partially purified zymogen, hydrolyzed the trypsin substrates BANA, BAEE, TAME and casein, and was inhibited by soybean > lima bean > ovomucoid trypsin inhibitors, and was also inhibited by TLCK. Calcium was required for optimal activity. The ratio of the rates of hydrolysis of BAEE and TAME by the active enzyme was 2.5:1 at 6 x 10-4 M final substrate concentration.

The active form of the zymogen appears to be acrosin (EC 3.4.21.10) and the zymogen can thus be called proacrosin.

 Accepted on August 23, 1974






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Copyright © 1975 by the Society for the Study of Reproduction.