A New Acrosin Inhibitor from Boar Spermatozoa
نویسندگان
چکیده
منابع مشابه
Boar acrosin. I. Purification and preliminary characterization of a proteinase from boar sperm acrosomes.
Acrosin is a proteolytic enzyme used by sperm to digest a path through the zona pellucida of the ovum. In ejaculated sperm it is inactivated by a proteinase inhibitor from seminal plasma that also inhibits trypsin. This inhibitor is removed or inactivated during the residence in the female reproductive tract as a part of the capacitation process. The boar acrosin-inhibitor complex was partially...
متن کاملDemonstration of acrosin in mouse spermatozoa.
Gelatinolytic activity of whole mouse spermatozoa was demonstrated by the gelatin film test. The presence of a trypsin-like protease (acrosin) in acidic extracts of mouse spermatozoa was shown by an electrophoretic method to separate the enzyme from a putative inhibitor.
متن کاملImmunocytochemical localization of acrosin in the anterior segment of the acrosomes of ram , boar and bull spermatozoa
Acrosin, a trypsin-like proteinase found in spermatozoa, is believed to play an essential role in fertilization by aiding the spermatozoon to penetrate the zona pellucida surrounding the egg (Mc Rorie and Williams, 1974). The precise cellular location of this enzyme is of considerable interest since such knowledge would aid in elucidating its mode of action. Biochemical studies have indicated t...
متن کاملBoar acrosin. II. Classification, inhibition, and specificity studies of a proteinase from sperm acrosomes.
Acrosin, a proteolytic enzyme located in the acrosome of sperm, exhibits amidase, esterase, and proteinase activity on synthetic and natural substrates containing arginyl and lysyl residues. Highly purified acrosin preparations from boar acrosomes have endopeptidase activity cleaving only the carboxyl bonds of arginine and lysine with a strong preference for arginine bonds. The Michaelis consta...
متن کاملProacrosin conversion inhibitor. Purification and initial characterization of a boar sperm protein which prevents the conversion of proacrosin into acrosin.
A proacrosin conversion inhibitor present in boar spermatozoa has been purified and initially characterized. Purification methods included sequential acid extractions of washed spermatozoa at pH 4.0, pH 3.5, and pH 2.5 followed by successive gel filtrations of the pH 2.5 sperm extract supernatant over Sephadex G-75 and G-50. The resulting 8.8-fold purified materials were judged to be homogeneou...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1982
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1982.tb06752.x