The major protamine from stallion sperm. Isolation and amino-acid sequence.
The major stallion protamine was isolated from sperm cell nuclei by extraction with 6M guanidine/5% mercaptoethanol, alkylation with 4-vinylpyridine and subsequent reversed-phase high-performance liquid chromatography. The primary structure of stallion protamine was determined by N-terminal sequencing of the intact protein and of the fragments obtained from thermolysin cleavage of the S-pyridylethylated and from endoproteinase Lys-C cleavage of the S-aminoethylated protein. Stallion protamine consists of 49 amino-acid residues and shows 49% identity with all other sequenced mammalian type 1 protamines.
Max-Planck-Institut für Biochemie, Martinsried bei München.
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D000085:Acetates; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006736:Horses; D006868:Hydrolysis; D008297:Male; D008969:Molecular Sequence Data; D011479:Protamines / Q000032:analysis*; D013094:Spermatozoa / Q000032:analysis*; D013820:Thermolysin
D000085:Acetates; D011479:Protamines; D013820:Thermolysin