Biol Reprod Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by MEIZEL, S.
Right arrow Articles by MUKERJI, S. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by MEIZEL, S.
Right arrow Articles by MUKERJI, S. K.
Agricola
Right arrow Articles by MEIZEL, S.
Right arrow Articles by MUKERJI, S. K.

Biology of Reproduction, Vol 14, 444-450, Copyright © 1976 by Society for the Study of Reproduction

Biochemical Studies of Proacrosin and Acrosin from Hamster Cauda Epididymal Spermatozoa

STANLEY MEIZEL 1, and SUDHIR K. MUKERJI 1

1 Department of human Anatomy, School of Medicine, University of California, Davis, California 95616


Partially purified proacrosin, the zymogen form of acrosin was obtained from unwashed hamster cauda epididymal spermatozoa by acid extraction and Sephadex column chromatography. Hamster proacrosin (92 percent of the total acrosin activity) and active acrosin (8 percent of the total activity) were eluted together with an apparent molecular weight of 70,000 ± 3000. However, the acrosin produced by complete "autoactivation" of the proacrosin preparation had an apparent molecular weight of 41,000 ± 3000. Hamster proacrosin "autoactivation" was a second order autocatalytic process typical of zymogen conversion to active enzyme. "Autoactivation" was most rapid at pH 8.0, accelerated by Ca2+ and inhibited by Zn2+. Our earlier studies have shown that rabbit sperm proacrosin had similar properties which suggests that the molecular nature of the two proacrosins is similar.

The following properties of hamster acrosin were similar to those of rabbit acrosin: pH optima; Km values with respect to TAME and BAEE; Ki's for p-aminobenzamidine and soybean trypsin inhibitor; and stimulation by Ca2+. Hamster acrosin was also inhibited by the following inhibitors known to inhibit rabbit acrosin: lima bean and ovomucoid trypsin inhibitors; the synthetic trypsin inhibitors TLCK, NPGB and benzamidine; and Zn2+. TPCK and L-arginine did not inhibit hamster or rabbit acrosins. Two striking differences between the two acrosins were: 1) hamster acrosin did not hydrolyze the rabbit acrosin substrate BANA: 2) the Vmax BAEE/Vmax TAME ratios of hamster and rabbit acrosins were 0.2 and 2.0 respectively.

The hydrolysis of the hamster egg zona pellucida by hamster sperm acrosin was demonstrated for the first time.

Note:
ACKNOWLEDGMENTS The authors wish to express their appreciation to Dr. Robert Erickson and Dr. Ryuzo Vanagimachi for providing us with their unpublished results. We are also grateful to Dr. B. Bavister for demonstrating egg collection techniques.

Submitted on November 21, 1975
Accepted on December 19, 1975




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
J. A. Foster, B. B. Friday, M. T. Maulit, C. Blobel, V. P. Winfrey, G. E. Olson, K.-S. Kim, and G. L. Gerton
AM67, a Secretory Component of the Guinea Pig Sperm Acrosomal Matrix, Is Related to Mouse Sperm Protein sp56 and the Complement Component 4-binding Proteins
J. Biol. Chem., May 9, 1997; 272(19): 12714 - 12722.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1976 by the Society for the Study of Reproduction.