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Primary structure of rabbit sperm protamine, the first protamine of its type with an aberrant N‐terminal
Author(s) -
Ammer H.,
Henschen A.
Publication year - 1988
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(88)80996-7
Subject(s) - protamine , thermolysin , protein primary structure , sperm , biochemistry , valine , amino acid , chemistry , biology , peptide sequence , microbiology and biotechnology , trypsin , enzyme , genetics , gene , heparin
Rabbit protamine was extracted from S ‐(pyridylethylated) sperm cell nuclei with hydrochloric acid and then isolated by reversed‐phase HPLC. The primary structure was determined by amino acid sequence analysis of the total protein and of fragments obtained by digestion with endoproteinase Lys‐C and thermolysin. The protamine contains 49 amino acid residues and is clearly homologous with mammalian type 1 protamines, 47% of the positions being invariant. Surprisingly, rabbit protamine possesses an N‐terminal valine residue, whereas all mammalian and several non‐mammalian protamine sequences of this type start with alanine, the N‐terminal region being remarkably conserved during evolution.