title: The primary structure of histone H2A from the sperm cell of the sea urchin Parechinus angulosus.
abstract: The 125 residues of the histone H2A from the sperm cells of the sea urchin Parechinus angulosus have been positioned. The N terminus is blocked by an acetyl group. Compared to the bovine histone, the sea urchin protein differs in 14 positions.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001974:Bromosuccinimide; D006657:Histones; D008297:Male; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D010669:Phenylthiohydantoin; D012617:Sea Urchins / Q000032:analysis*; D013094:Spermatozoa / Q000032:analysis*; D013820:Thermolysin; D014357:Trypsin
chemical_list: D006657:Histones; D010446:Peptide Fragments; D010669:Phenylthiohydantoin; D010447:Peptide Hydrolases; D014357:Trypsin; D013820:Thermolysin; D001974:Bromosuccinimide