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Journal of Lipid Research, Vol 36, 1147-1151, Copyright © 1995 by Lipid Research, Inc.

ARTICLES

Highly efficient immobilization of phospholipase A2 and its biomedical applications

Z Shen and W Cho
Department of Chemistry (M/C 111), University of Illinois, Chicago 60607-7061, USA.

A new method for the immobilization of phospholipase A2 (PLA2) has been developed to enhance the activity retention of immobilized PLA2. When PLA2 from the venom of Agkistrodon piscivorus piscivorus was pretreated with 4-nitro-3-octanoyl-oxybenzoic acid to acylate epsilon-amino groups of two lysines (Lys-7 and Lys-10) and the resulting acylated enzyme was covalently coupled onto carbonyldiimidazole-activated cross-linked agarose beads, the immobilized acylated enzyme showed high retention of activity toward various aggregated phospholipids. Toward densely packed phospholipid bilayers, such as large unilamellar vesicles of 1- palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, the immobilized acylated A. p. piscivorus PLA2 was 25-fold more active than the soluble A. p. piscivorus PLA2. The general applicability of our immobilization protocol was demonstrated by the high retention of activity achieved for the immobilized acylated PLA2 from the venom of Naja naja naja. In particular, full activity retention of the immobilized acylated A. p. piscivorus PLA2 toward phospholipids on the surface of human low density lipoproteins suggests its potential usefulness in a newly developed PLA2-based therapy for hypercholesterolemia.
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This article has been cited by other articles:

				S. K. Han, E. T. Yoon, D. L. Scott, P. B. Sigler, and W. Cho Structural Aspects of Interfacial Adsorption. A CRYSTALLOGRAPHIC AND SITE-DIRECTED MUTAGENESIS STUDY OF THE PHOSPHOLIPASE A2 FROM THE VENOM OF AGKISTRODON PISCIVORUS PISCIVORUS J. Biol. Chem., February 7, 1997; 272(6): 3573 - 3582. [Abstract] [Full Text] [PDF]