Isolation and Fundamental Properties of a Phospholipase A2 Inhibitor from the Blood Plasma of Trimeresurus flavoviridis

Phospholipase A2 inhibitor was purified from the blood plasma of Habu, Trimeresurus flavoviridis, by Sephadex G-200 gel filtration, DEAE-cellulose chromatography, and Blue-Sepharose CL-6B column chromatography. The purified inhibitor was shown to be a glycoprotein with a molecular weight of about 10...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1989-12, Vol.106 (6), p.966-971
Main Authors: Kogaki, Hiroyuki, Inoue, Seiji, Ikeda, Kiyoshi, Samejima, Yuji, Omori-Satoh, Tamotsu, Hamaguchi, Kozo
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Chromatography, Gel
Dose-Response Relationship, Drug
Fundamental and applied biological sciences. Psychology
Glycoproteins
Glycoproteins - blood
Glycoproteins - isolation & purification
Kinetics
Phospholipases - antagonists & inhibitors
Phospholipases A - antagonists & inhibitors
Phospholipases A - blood
Phospholipases A - isolation & purification
Phospholipases A2
Proteins
Sepharose - analogs & derivatives
Snakes - blood
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Summary:Phospholipase A2 inhibitor was purified from the blood plasma of Habu, Trimeresurus flavoviridis, by Sephadex G-200 gel filtration, DEAE-cellulose chromatography, and Blue-Sepharose CL-6B column chromatography. The purified inhibitor was shown to be a glycoprotein with a molecular weight of about 100K. It was found to consist of four subunits whose molecular weights were around 20–24K. In order to examine the inhibition mechanism of the inhibitor, the interaction of the inhibitor with a phospholipase A2 from T. flavoviridis venom was examined by Sephadex G-100 gel filtration. One inhibitor molecule was found to bind directly to one phospholipase A2 molecule in both the presence and absence of Ca2+. The inhibitor inhibited the phospholipase A2 from T. flavoviridis venom with an apparent dissociation constant, K1, of 1.7×l0−10 M, but not the porcine pancreas enzyme or the Agkistrodon halys blomhoffii enzyme belonging to the same family, Crotalidae, as T. flavoviridis, or the phospholipase C from Bacillus cereus.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122983