Boar acrosin. Association of an endogenous membrane proteinase with phospholipid membranes.
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 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...
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Proacrosin, the zymogen precursor of acrosin, was shown to associate with anionic phospholipid membranes through apparent electrostatic charge interactions. This association was diminished by elevated cation concentrations and was dependent on membrane composition, as shown both by direct binding assays and by following the phospholipid stimulation of conversion of proacrosin into acrosin.
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Fusion of multilamellar phospholipid vesicles with planar phospholipid bilayer membranes was monitored by the rate of appearance in the planar membrane of an intrinsic membrane protein present in the vesicle membranes. An essential requirement for fusion is an osmotic gradient across the planar membrane, with the cis side (the side containing the vesicles) hyperosmotic to the opposite (trans) s...
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To characterize the specificity of zinc binding to phospholipid membranes in terms of headgroup structure, hydration and phase behavior we studied the zwitterionic lipid 1-palmitoyl-2-oleoyl-phosphatidylcholine as a function of hydration at 30 degreesC in the presence and absence of ZnCl2. Zinc forms a 2:1-1:1 complex with the lipid, and in particular with the negatively charged phosphate group...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)69256-2