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J. Biochem, 1988, Vol. 104, No. 3 326-328
© 1988 Japanese Biochemical Society

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Amino Acid Composition and NH2-Terminal Amino Acid Sequence of Human Phospholipase A2 Purified from Rheumatoid Synovial Fluid1

Shuntaro Hara*, Ichiro Kudo*, Kunio Matsuta**, Terumasa Miyamoto** and Keizo Inoue*

*Department of Health Chemistry, Faculty of Pharmaceutical Sciences
**Department of Medical and Physical Therapy, Faculty of Medicine, The University of Tokyo Bunkyo-ku, Tokyo 113

The amino acid composition and partial NH2-terminal amino acid sequence of an extracellular phospholipase A2 in human rheumatoid synovial fluid were determined. The predominant amino acids in the phospholipase A2 were cysteine, glycine, arginine, and lysine, suggesting that it is a basic one. The NH2-terminal 34 amino acids were found to be as follows:

Asn-Leu-Val-Asn-Phe-His-Arg-Met-Ile-Lys-Leu-Thr-Thr-Gly-Lys-Glu-Ala-Ala-Leu-Ser-Tyr-Gly-Phe-Tyr-Gly-Cys-X-Cys-Gly-Val-Gly-Gly-Arg-Gly

The enzyme contains Phe-5, Met-8, Ile-9, Tyr-24, Gly-25, Cys-26, Cys-28, Gly-29, Gly-31, Gly-32, and Gly-34 residues, all of which are conserved in most of the sequenced phospholipase A2 The remarkable feature of this enzyme was the absence of Cys-11, which is conserved in the "Group I" enzyme family. This is the first report concerning partial amino acid sequences of human non-pancreatic phospholipase A2.

1This work was supported in part by Grant-in-Aid for Scientific Research (Nos. 62624504 and 62870093) from the Ministry of Education, Science and Culture of Japan.


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