Proteolytic degradation of protamine during thiol-induced nuclear decondensation in rabbit spermatozoa.
Rabbit sperm nuclei decondensed when incubated with dithiothreitol and Triton X-100. Protamine isolated from these nuclei during the course of treatment exhibited marked and progressive degradation. Timed interval experiments revealed that the degradation of protamine significantly preceded sperm nuclear decondensation and reached its maximum extent before decondensation was completed. Studies with protease inhibitors demonstrated that proteolysis was involved in both nuclear decondensation and protamine degradation.
D000818:Animals; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism; D004229:Dithiothreitol / Q000494:pharmacology; D008297:Male; D010447:Peptide Hydrolases / Q000494:pharmacology*; D011092:Polyethylene Glycols / Q000494:pharmacology; D011479:Protamines / Q000378:metabolism*; D011817:Rabbits; D013094:Spermatozoa / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013997:Time Factors; D014361:Trypsin Inhibitors / Q000494:pharmacology
D011479:Protamines; D013438:Sulfhydryl Compounds; D014361:Trypsin Inhibitors; D011092:Polyethylene Glycols; D010447:Peptide Hydrolases; D004229:Dithiothreitol