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Biology of Reproduction, Vol 3, 275-282, Copyright © 1970 by Society for the Study of Reproduction
1 Division of Reproductive Biology, Department of Obstetrics and Gynecology, University of
Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 Methods are described for the isolation of subcellular fractions from rabbit, rhesus monkey, and human sperm using sucrose-density gradients. All three species were found to
possess hyaluronidase and a specific trypsin-like enzyme in the head fractions from their
spermatozoa. Both enzymes were further localized in the acrosomes in the rabbit and rhesus
monkey, and were found to be present in a relatively constant ratio in all three species,
although the specific activities do vary between species. A chymotrypsin like enzyme, present in ejaculated but not in the epididymal sperm, was extracted in the soluble portion of the
spermatozoa and apparently originates by adsorption from the seminal plasma. The cyclic
changes in human cervical mucus alpha1-antitrypsin were found to be without any apparent
physiologic function in relation to the acrosomal trypsin-like enzyme or the seminal plasma
chymotrypsin-like enzyme, since the inhibitor was ineffective on both enzymes.
This article has been cited by other articles:
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L. J. D. Zaneveld, B. M. Dragoje, and G. F. B. Schumacher Acrosomal Proteinase and Proteinase Inhibitor of Human Spermatozoa Science, August 25, 1972; 177(4050): 702 - 703. [Abstract] [PDF] |
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