Autor: |
Sautière, Pierre, Briand, Gilbrt, Gusse, Michel, Chevaillier, Philippe |
Předmět: |
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Zdroj: |
European Journal of Biochemistry; 10/1/81, Vol. 119 Issue 2, p251-255, 5p |
Abstrakt: |
A protamine was isolated from mature sperm nuclei of the dog-fish Scylliorhinus caniculus. It contains 31 amino acids per molecule and only five types of residues: arginine (20), glycine (6), serine (3), alanine (1) and tyrosine (1). The primary structure of this protamine is reported. The N-terminal sequence contains the four hydroxylated amino acids of the molecule; the C-terminal region shows a sequence of eleven adjacent residues of arginine and contains all the glycine residues present in the protein. The structure of this `scylliorhinine' is compared to the amino acid sequence of other sperm protamines whose structure has been previously published. The presence of a modified tyrosinc residue in some preparations is discussed in relation to sperm maturation. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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