Characterization of cockroach (Periplaneta americana) fat body phospholipase A(2) activity.
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 microM 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 degrees 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.
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Department of Zoology, The University of Western Ontario, London, Canada.
Steele
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JE
D000818:Animals; D002118:Calcium / Q000378:metabolism; D005216:Fat Body / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D010526:Periplaneta / Q000201:enzymology*; D010713:Phosphatidylcholines / Q000378:metabolism; D010741:Phospholipases A / Q000378:metabolism*; D013379:Substrate Specificity
D010713:Phosphatidylcholines; D010741:Phospholipases A; D002118:Calcium