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• W2155753756 abstract "A nuclear basic protein, galline, could be isolated efficiently from semen of the domestic rooster by a method which has been used for preparing protamines from fish sperm. The molecular weight of whole galline was estimated to be about 7,000 as hydrochloride by gel chromatography on Sephadex G-75 and the sedimentation coefficient was calculated to be 0.74 S by sedimentation velocity method. Whole galline was separated into eight main fractions by ion-exchange chromatography on Bio-Gel CM-30, and each fraction was characterized by means of amino acid and end groups analyses. Three fractions (G-I, G-V and G-VI) of them have thus been confirmed to be almost homogenous and ready for structural studies, and the homogeneity of these three fractions was shown by polyacrylamide disk electrophoresis. The following formulae were obtained based on the amino acid composition and analyses of end groups and terminal sequences. G-I: H-Ser-(Ser2, Gly3, Val, Tyr, Arg14·1)-Tyr-OH; G-V: H-Ala-Arg-Tyr-(Ar2, Ser, Gly)-(Thr, Ser7, Pro2, Gly2, Tyr, Arg20·1)-Ala-Arg-Arg-OH; G-VI: H-Ala-Argn-Tyr-(Arg4-n, Ser, Gly)-(Thr, Ser7, Pro2, Gly2, Tyr, Arg22·1)-Ala-Ser-Arg-Arg-Arg-OH (n = 1–4)." @default.
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• W2155753756 date "2009-01-12" @default.
• W2155753756 modified "2023-09-23" @default.
• W2155753756 title "STUDIES ON A PROTAMINE (GALLINE) FROM FOWL SPERM: 1. Fractionation and Some Characterization" @default.
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• W2155753756 doi "https://doi.org/10.1111/j.1399-3011.1973.tb02330.x" @default.
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