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J. Biochem, 1988, Vol. 104, No. 5 767-772
© 1988 Japanese Biochemical Society

research-article

The Primary Structure of Rat Platelet Phospholipase A21

Makio Hayakawa*, Ichiro Kudo*,2, Motowo Tomita**, Shoshichi Nojima*,3 and Keizo Inoue*

*Department of Health Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Bunkyo-ku, Tokyo 113
**Faculty of Pharmaceutical Sciences, Showa University Shinagawa-ku, Tokyo 143

2 To whom correspondence should be addressed

In our previous report (Hayakawa, M., Kudo, I., Tomita, M., & Inoue, K. (1988) J. Biochem. 103, 263–266), we have shown that phospholipases A2 purified from rat platelet membrane fractions and an extracellular medium of thrombin-stimulated rat platelets were essentially identical to each other. Both purified enzymes were digested with proteases, and the resulting peptides were subjected to primary sequence determination. The sequence analysis of the HPLC-separated peptides and the alignment of the sequences showed a tentative primary structure of rat platelet phospholipase A2, which was composed of 125 amino acid residues. It showed 47% homology with snake venom Agkistrodon halys blomhoffii phospholipase A2.

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.

3 Present address: Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko-machi, Kanagawa 199-01.


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