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Biology of Reproduction, Vol 6, 87-97, Copyright © 1972 by Society for the Study of Reproduction
1 Department of Anatomy, University of Hawaii School of Medicine, Honolulu, Hawaii 96822 A silver proteinate method developed by Takamatsu et al. (1963) was employed for
visual demonstration of the active sites of proteinase in the spermatozoa of nine mammalian
species (golden hamster, mouse, deer mouse, rat, guinea pig, rabbit, dog, bull, and human)
and one avian species (cock). Proteinase activity was demonstrated only in the acrosomal
caps of all mammalian species studied. Strong proteinase activity was observed in the acrosomes of cock spermatozoa. In the golden hamster, activity was demonstrated in the acrosomes of not only mature spermatozoa, but also of immature spermatozoa as well as early
spermatids. The optimum activity of the acrosomal proteinase in all of these species was generally
in the acidic range. Studies using golden hamster and rabbit spermatozoa showed that proteinase activity was not inhibited by soybean and lima bean trypsin inhibitors, but it was
drastically inhibited by tetrabutylammonium iodide, and completely inhibited by HgCl2,
KCN, KMnO4, heparin sodium salt, phosphorylated hesperidin and a hydroquinone sulphonic acid-formaldehyde polymer. It was inferred that the hamster and rabbit sperm
acrosomal proteinase demonstrable by this technique represents a proteinase conjugated
with hyaluronidase. The function of such a proteinase was judged to be depolymerization
of the matrix of the cumulus oophorus in close association with the action of hyaluronidase.
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