Isolation and characterization of a phospholipase A2 inhibitor from the blood plasma of the Thailand cobra Naja naja kaouthia.
A phospholipase A2 (PLA2) inhibitory protein was purified from the blood plasma of the Thailand cobra Naja naja kaouthia by sequential chromatography on Sephadex G-200, DEAE Affi-Gel Blue, and Protein-Pak G-Butyl columns. The purified inhibitor was a glycoprotein with an apparent molecular mass of about 90 kDa and contained 25- and 31-kDa subunits with a molar ratio of 1:2. The 31-kDa subunit contained a glycosidic chain and the molecular mass was reduced to 28 kDa by N-glycosidase F treatment. The amino acid compositions of the two subunits were characterized by their high content of cysteine residues. The inhibitor inhibited group II as well as group I PLA2's. Since the fundamental properties were different from those of the two Crotalidae inhibitors already reported, the cobra inhibitor might be a new type of PLA2 inhibitor.
Ohkura
N
N
Department of Biochemistry, Osaka University of Pharmaceutical Sciences, Japan.
Inoue
S
S
Ikeda
K
K
Hayashi
K
K
D017836:Agkistrodon; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D017815:Elapidae / Q000097:blood*; D004791:Enzyme Inhibitors / Q000097:blood / Q000737:chemistry; D006023:Glycoproteins / Q000097:blood / Q000737:chemistry; D008970:Molecular Weight; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D011487:Protein Conformation; D013045:Species Specificity; D017841:Trimeresurus
D000596:Amino Acids; D004791:Enzyme Inhibitors; D006023:Glycoproteins; D010741:Phospholipases A; D054467:Phospholipases A2