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Purification and characterization of human platelet phospholipase A 2 which preferentially hydrolyzes an arachidonoyl residue
Author(s) -
Takayama Kiyoshi,
Kudo Ichiro,
Kim Dae Kyong,
Nagata Koichi,
Nozawa Yoshinori,
Inoue Keizo
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80506-x
Subject(s) - biochemistry , phospholipase , residue (chemistry) , phosphatidylcholine , chemistry , phospholipase a1 , enzyme , phospholipase c , phospholipase a , phospholipase a2 , molecular mass , hydrolysis , phospholipase d , phospholipid , chromatography , membrane
A phospholipase A 2 with an arachidonoyl residue preference was purified about 11 700‐fold from human platelet soluble fraction to near homogeneity. The purified phospholipase A 2 exhibited a molecular mass of about 90 kDa on SDS polycrylamide gel electrophoresis and hydrolyzed phospholipids with a arachidonoyl residue more effectively than those with a linoleoyl residue. The catalytic activity of the purified enzyme detected with phosphatidylcholine as a substrate increased sharply between 3 × 10 −7 and 10 −6 M free calcium ion. Thus, the 90‐kDa phospholipase A 2 is considered to be a novel enzyme, distinct from the 14‐kDa one previously purified from human platelets. The 90‐kDa phospholipase A 2 may participate mainly in arachidonate metabolism of platelets.