Primary structure of rabbit sperm protamine, the first protamine of its type with an aberrant N-terminal.
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.
Ammer
H
H
Max Planck Institute for Biochemistry, Martinsried, FRG.
Henschen
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases; D008297:Male; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011479:Protamines / Q000302:isolation & purification; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid; D013094:Spermatozoa / Q000032:analysis*; D013820:Thermolysin
D000596:Amino Acids; D010446:Peptide Fragments; D011479:Protamines; D010450:Endopeptidases; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase; D013820:Thermolysin