Activity and subcellular localization of proteolytic enzymes of boar and rabbit spermatozoa.
Comparison of the mode and time course of depolymerization of the gelatin by boar and rabbit spermatozoa obtained from the ejaculates and the female reproductive tract revealed that the proteolytic activity of the spermatozoa was not changed during their passage through the female reproductive tract. In all sperm samples the depolymerization started at the level of the equatorial segment, proceeded to the apical part and digested the substrate around the sperm head. The time course of depolymerization was also the same in all samples. Slight differences were caused by degeneration changes affecting the acrosomal region of the sperm head and accelerating the initial course of substrate depolymerization. The results were confirmed by investigating the state of the acrosomes of individual sperm samples using the silver proteinate method. It appeared that samples with greater numbers of spermatozoa with damaged acrosome begin to affect the substrate a few minutes earlier. The disadvantage of the methods used is that the release of the proteolytic enzymes from the sperm head is probably caused by postmortem degeneration changes of the spermatozoa.
D000177:Acrosome / Q000378:metabolism; D000818:Animals; D005780:Gelatin; D008297:Male; D008722:Methods; D010447:Peptide Hydrolases / Q000378:metabolism*; D011817:Rabbits / Q000502:physiology*; D013077:Sperm Head / Q000201:enzymology; D013094:Spermatozoa / Q000378:metabolism*; D013552:Swine / Q000502:physiology*; D013997:Time Factors
D005780:Gelatin; D010447:Peptide Hydrolases