Biol Reprod Track the topics, authors and articles important to you
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 Google Scholar
Google Scholar
Right arrow Articles by SRIVASTAVA, P. N.
Right arrow Articles by GOULD, K. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by SRIVASTAVA, P. N.
Right arrow Articles by GOULD, K. G.
Agricola
Right arrow Articles by SRIVASTAVA, P. N.
Right arrow Articles by GOULD, K. G.

Biology of Reproduction, Vol 25, 363-369, Copyright © 1981 by Society for the Study of Reproduction

Studies on Hydrolytic Enzymes of Chimpanzee Semen

PRAKASH N. SRIVASTAVA 1, AKHLAQ A. FAROOQUI 1, , and KENNETH G. GOULD 2

1 Department of Biochemistry, University of Georgia, Athens, Georgia 30602
2 Reproductive Biology Section, Yerkes Regional Primate Research Center, Emory University, Atlanta, Georgia 30322


The distribution of lysosomal hydrolases in sperm acrosomes and seminal plasma was studied in semen samples (n = 9) obtained from six chimpanzees by automasturbation. Most of the hydrolytic enzymes can be extracted by the MgCl2, step from spermatozoa. beta-N-Acetylhexosaminidase and hyaluronidase showed highest specific activity in the MgCl2 extract. The specific activities of arylsulfatase, beta-glucuronidase, and agr-L-fucosidase were 4-8 times higher in the detergent extract. The seminal plasma showed high activities of acid and alkaline phosphatases and low specific activity of beta-galactosidase. The acidic forms of these enzymes predominated in the seminal plasma as shown both by the DEAE-cellulose chromatography and polyacrylamide gel electrophoresis. Concanavalin A Sepharose chromatography confirmed the glycoprotein nature of these enzymes and gave 2-25-fold purification.

Note:
ACKNOWLEDGMENTS The authors thank Mrs. Elaine Foster for her skillful technical assistance and Mr. Jim Faulkner for providing chimpanzee semen. The work was supported by NIH Grants HD 14947-01 and RR00165, and by Ford Foundation Grant 690-0645.

Submitted on January 26, 1981
Accepted on May 6, 1981






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1981 by the Society for the Study of Reproduction.