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Purification and characterization of two basic spermatid‐specific proteins isolated from the dog‐fish Scylliorhinus caniculus
Author(s) -
Chauviere Muriel,
Laine Bernard,
Sautiere Pierre,
Chevaillier Philippe
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80386-x
Subject(s) - protamine , spermatid , cysteine , hydrolysate , biochemistry , histone , chemistry , amino acid , amino acid analysis , fish <actinopterygii> , hydrolysis , chromatography , biology , dna , enzyme , botany , sperm , heparin , fishery
In dog‐fish spermatid nuclei two intermediate proteins S 1 and S 2 replace histones before the setting down of protamines. These spermatid‐specific proteins were isolated by carboxymethyl‐cellulose chromatography and purified by high pressure liquid chromatography. S 1 and S 2 are characterized by a high content of basic residues and by the lack of cysteine and phenylalanine. The determination of their amino acid composition and of their N‐ and C‐terminal sequences prove that each protein corresponds to a specific molecule which can be considered neither as a histone hydrolytic product nor as a protamines precursor.