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J. Biochem, 1988, Vol. 103, No. 2 263-266
© 1988 Japanese Biochemical Society

research-article

Purification and Characterization of Membrane-Bound Phospholipase A2 from Rat Platelets1

Makio Hayakawa, Faculty of Pharmaceutical Sciences*, Ichiro Kudo, Faculty of Pharmaceutical Sciences*, Motowo Tomita, Faculty of Pharmaceutical Sciences** and Keizo Inoue, Faculty of Pharmaceutical Sciences*,2

* Department of Health Chemistry, The University of Tokyo Bunkyo-ku, Tokyo 113
** Showa University Shinagawaku, Tokyo 143

2 To whom correspondence should be addressed.

Phospholipase A2 was solubilized from rat platelet membrane by 1 M KC1 and purified to near homogeneity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and HPLC. The characteristics of the purified membrane-bound enzyme were compared with those of phospholipase A2 released from thrombin-stimulated rat platelets (Horigome, K., Hayakawa, M., Inoue, K., & Nojima, S. (1987) J. Biochem. 101, 625–631). The molecular weights, elution profiles on reversed-phase HPLC, and NH2-terminal sequences were identical for the two enzymes. Other characteristics of the two enzymes, such as specific activity, substrate specificity, pH optimum, Ca2+ requirement, heat lability, and sensitivity to p-bromophenacyl bromide were also indistinguishable. These findings suggest that both enzymes share a common structure.

1 This work was supported in part by Grants-in-Aid for Scientific Research (Nos. 61106008 and 62870093) from the Ministry of Education, Science and Culture of Japan.


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