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Characterization of cockroach (Periplaneta americana) fat body phospholipase A2 activity

✍ Scribed by D. Sun; J.E. Steele

Publisher: John Wiley and Sons
Year: 2002
Tongue: English
Weight: 192 KB
Volume: 49
Category: Article
ISSN: 0739-4462
DOI: 10.1002/arch.10014

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✦ Synopsis

Abstract

A phospholipase has been identified in the fat body of the American cockroach, Periplaneta americana, which removes fatty acid from the sn‐2 acyl position of an artificial substrate. The enzyme has been characterized using a crude preparation obtained by low‐speed centrifugation of the homogenized tissue. With 1‐hexadecanoyl‐2‐(1‐pyrenedecanoyl)‐sn‐glycero‐3‐phosphocholine as the substrate, the K~m~ has been estimated to be 1.17 μM and the v~max~ 113.5 pmol/min/mg protein. The phospholipase has a pH optimum close to 7 and shows maximal activity at 50°C. Activity of the phospholipase has been determined in cytosolic and plasma membrane fractions. The specific activity of the latter fraction is approximately twice that of the cytosol. The enzyme in both fractions is Ca^2+^‐independent. Arch. Insect Biochem. Physiol. 49:149–157, 2002. © 2002 Wiley‐Liss, Inc.

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