Amino acid sequences of the two subunits of a phospholipase A2 inhibitor from the blood plasma of Trimeresurus flavoviridis. Sequence homologies with pulmonary surfactant apoprotein and animal lectins.

摘要: Phospholipase A2 inhibitor (PLI), purified from the blood plasma of Habu snake (Trimeresurus flavoviridis), was separated into two distinct subunits, PLI-A and PLI-B. These subunits were shown to be glycoproteins with molecular weights around 21,000-22,000. When they deglycosylated chemically trifluoromethanesulfonic acid, found 17,000. Their amino acid sequences determined by alignment peptides obtained lysyl endopeptidase digestion Staphylococcus aureus V8 protease digestion. PLI-B each composed 147 residues one residue, Asn103, being for N-linked glycosylation, their protein portions calculated 16,368 16,408, respectively. Each subunit contained four cysteine residues, all which exist in disulfide linkages (Cys64-Cys141 Cys119-Cys133). The showed 89.9% homology other. compared those lipocortins, no significant homologies detected. But significantly homologous COOH-terminal carbohydrate recognition pulmonary surfactant apoprotein animal lectins.