THE ISOLATION AND CHARACTERIZATION OF A 3RD OR NEUTRAL PHOSPHOLIPASE-A2 IN THE VENOM OF AGKISTRODON-HALYS-BLOMHOFFII - AN IMPROVED FRACTION PROCEDURE FOR ALL 3 ENZYMES
THE ISOLATION AND CHARACTERIZATION OF A 3RD OR NEUTRAL PHOSPHOLIPASE-A2 IN THE VENOM OF AGKISTRODON-HALYS-BLOMHOFFII - AN IMPROVED FRACTION PROCEDURE FOR ALL 3 ENZYMES
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DOI：
10.1016/0005-2760(80)90113-7
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发表时间：
1980-01-01
期刊：
影响因子：
--
通讯作者：
MORALES, R
中科院分区：
文献类型：
--
作者：
HANAHAN, DJ;JOSEPH, M;MORALES, R
The isolation of a new, 3rd phospholipase A2 from A. halys blomhoffii is described. On the basis of a pI [isoelectric point] value of 6.9, it is termed a neutral phospholipase A2. It was characterized as to its amino acid content, activity towards phosphatidylcholine, heat stability and hemolytic behavior on human erythrocytes. A comparison of these characteristics with those of the acidic and basic phospholipases A2 established the uniqueness of the neutral enzyme. Two particularly important observations were concerned with the complete stability of the 3 phospholipases on heating at 100.degree. C at pH 6.0 in the presence of 10 mM Ca2+, but variable stability in the absence of Ca2+, and the significant lack of hemolytic activity by the acidic (pI 4.9) phospholipase A2 as compared to the neutral (pI 6.9) and basic (pI 8.7) enzyme which produced extensive hemolysis of human erythrocytes. Other facets of the characteristics of these phospholipases are discussed.
