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J. Biochem, 1989, Vol. 106, No. 1 38-42
© 1989 Japanese Biochemical Society

research-article

Multiple Forms of Phospholipase A2 in Arthritic Synovial Fluid

Jeffrey J. Seilhamer*,1, Shelley Plant*, Waldemar Pruzanski**, James Schilling*, Eva Stefanski**, Peter Vadas** and Lorin K. Johnson*

*California Biotechnology Inc. 2450 Bayshore Parkway, Mt. View, CA 94043, U.S.A
**The Wellesley Hospital, University of Toronto Toronto, Ontario, M4Y 1J3 Canada

1To whom correspondence should be addressed. Present address: Ideon Corporation, 515 Galveston Dr., Redwood City, CA 94063, U.S.A.

Phospholipase A2 (PLA2) has been purified to homogeneity from human arthritic synovial fluid. The activity resolved into multiple peaks by preparative HPLC. The most abundant peak (A) was present in synovial fluid from patients with rheumatoid arthritis, osteoar-thritis, and psoriatic arthritis. A second major peak (B) was variable and lower in relative abundance, but was distinguishable from peak A by its stimulated activity in the presence of either 0.5 M Tris or 0.1% sodium deoxycholate (DOC), in addition to its longer HPLC column retention time. Both peaks required Ca2+ and showed optimal activity in DOC/ phosphatidylcholine (PC) mixed micelle assays between pH 8.0 and 9.0. Both peaks showed higher activity with PC as substrate than with PI, however peak A exhibited higher activity with PE than PC. Upon preparative SDS-polyacrylamide gel electrophoresis, both peaks of PLA2 activity were resolved as proteins of approximately 14, 000 Da. The N-terminal sequence obtained from purified peak A material matched that of a recent similar isolate (Hara et al. (1988))


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