title: Partial primary structure of human alpha 2-antiplasmin-homology with other plasma protease inhibitors.
abstract: Human alpha 2-antiplasmin was digested with trypsin and with chymotrypsin and about 70 percent of the amino acids were sequenced and aligned in peptides ranging from 2 to 33 residues. Here we report five sequences of 21 to 33 residues. When these were compared with the primary structures of antithrombin III, alpha 1-antitrypsin and ovalbumin, which belong to the same protein superfamily (Hunt and Dayhoff [1980] Biochem Biophys Res Commun 95: 864-871), three peptides showed clear homologies with these proteins, indicating that alpha 2-antiplasmin also belongs to that superfamily. In addition, alpha 2-antiplasmin appeared to contain at least one internal homology.
mesh_terms: D000595:Amino Acid Sequence; D000990:Antithrombin III / Q000032:analysis; D006801:Humans; D010047:Ovalbumin / Q000032:analysis; D010455:Peptides / Q000032:analysis; D011480:Protease Inhibitors / Q000032:analysis*; D000515:alpha 1-Antitrypsin / Q000032:analysis; D000979:alpha-2-Antiplasmin / Q000032:analysis*
chemical_list: D010455:Peptides; D011480:Protease Inhibitors; D000515:alpha 1-Antitrypsin; D000979:alpha-2-Antiplasmin; D000990:Antithrombin III; D010047:Ovalbumin