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It was found that phospholipase A2 and lysophospholipase, both of which were released from thrombin-stimulated rat platelets, had high affinity to insolubilized heparin. Phospholipase A2 released from rat platelets was purified by the sequential use of column chromatography on heparin-Sepharose and TSK gel G2000SW (high-performance liquid chromatography, HPLC). The enzyme was near homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and HPLC, and its Mr was estimated to be 13,500. The purified enzyme was labile and lost its activity within 1 h when incubated at 37 degrees C. Phospholipids or detergent in the solution protected the enzyme against inactivation. Phospholipase activity was inhibited by p-bromophenacylbromide, but not by diisopropylfluorophosphate or iodoacetamide. Lysophospholipase, which was also released from rat platelets, was separated from phospholipase A2 by chromatography on heparin-Sepharose.
K Horigome, and
M Hayakawa, and
K Inoue, and
S Nojima
February 1988,
Journal of biochemistry,
K Horigome, and
M Hayakawa, and
K Inoue, and
S Nojima
March 1988,
Journal of biochemistry,
K Horigome, and
M Hayakawa, and
K Inoue, and
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September 1990,
Biochimica et biophysica acta,
K Horigome, and
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K Horigome, and
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January 1991,
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K Horigome, and
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December 1993,
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K Horigome, and
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January 1991,
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K Horigome, and
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January 1989,
Journal of lipid mediators,
K Horigome, and
M Hayakawa, and
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January 1990,
Advances in prostaglandin, thromboxane, and leukotriene research,
K Horigome, and
M Hayakawa, and
K Inoue, and
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October 1992,
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