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- W1969247068 abstract "1. Sperm nuclei were isolated and purified from boar semen by a procedure involving differential solubilization of sperm tail and acellular materials by brief exposure to reducing reagent in the presence of cationic detergent, and sedimentation through 60% sucrose. The weight ratio of DNA:RNA: total protein: protamine in this preparation was 1.00: 0.02: 1.05: 0.75, and the molar ratio of phosphorus to arginine was 1.12. 2. Boar protamine was extracted with cold acid from ethanol precipitate of reduced and carboxymethylated nuclei in 6 M guanidine hydrochloride and purified by ion-exchange chromatography on CM-cellulose. The molecular weight of the protamine was estimated to be 6600 by the gel filtration method. The protamine consisted of a single amino terminus alanine and either half-cystine or arginine as carboxy terminus, and was composed of Thr, Ser3, Pro2, Ala2, Val2, Ile, His, Half-cystine9-10 and Arg26 . 3. Chymotryptic digestion gave rise to a single amino-terminal peptide, Ala-Arg-Tyr, and two carboxy-terminal peptides, Thr-Val-Ile-Arg-Cys-Arg2-Cys and Thr-Val-Ile-Arg-Cys-Arg2, which confirmed the heterogeneity of the protamine at the carboxy-terminal end." @default.
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- W1969247068 date "1982-10-01" @default.
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- W1969247068 title "Isolation and characterization of nuclear basic protein (protamine) from boar spermatozoa" @default.
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- W1969247068 doi "https://doi.org/10.1016/0167-4838(82)90358-2" @default.
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