Purification and characterization of two basic spermatid-specific proteins isolated from the dog-fish Scylliorhinus caniculus |
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Authors: | M Chauviere B Laine P Sautiere P Chevaillier |
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Affiliation: | Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England |
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Abstract: | In dog-fish spermatid nuclei two intermediate proteins S1 and S2 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. S1 and S2 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. |
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Keywords: | Oligosaccharide conformation Nuclear Overhauser effect Human serum transferin Two-dimensional NMR spectroscopy |
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