Purification of a novel calcium-independent phospholipase A2 from rabbit kidney

60Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

We have recently identified a cytosolic calcium-independent phospholipase A2 (PLA2) that represents the major measurable PLA2 activity in rabbit proximal tubules (Portilla, D., Shah, S. V., Lehman, P. A., and Creer, M. H. (1994) J. Clin. Invest. 93, 1609-1615). We now report the 3200- fold purification of this PLA2 to homogeneity from rabbit kidney cortex through sequential column chromatography including anion exchange, hydrophobic interaction, Mono Q, hydroxylapatite, phenyl-Sepharose, and chromatofocusing fast protein liquid chromatography from rabbit kidney cortex. The purified enzyme had a molecular mass of 28 kDa, possessed a specific activity of 1.2 μmol/mg min and a neutral pH optimum, and exhibited a preferential hydrolysis toward sn-2 fatty acid from diradylglycerophospholipids. The purified polypeptide hydrolyzed plasmenylcholine > phosphatidylcholine glycerophospholipids and selectively cleaved phospholipids containing arachidonic acid at the sn-2 position in comparison to oleic acid. Antibodies against the purified protein precipitated all of the soluble calcium-independent PLA2 activity from rabbit kidney cortex. These data altogether suggest that the 28-kDa protein in the kidney represents a novel class of calcium-independent PLA2.

Cite

CITATION STYLE

APA

Portilla, D., & Dai, G. (1996). Purification of a novel calcium-independent phospholipase A2 from rabbit kidney. Journal of Biological Chemistry, 271(26), 15451–15457. https://doi.org/10.1074/jbc.271.26.15451

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free