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Plant Physiology 69:1293-1297 (1982)
© 1982 American Society of Plant Biologists

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Articles

Solubilization and Characterization of an Acyl-Coenzyme A 1

O-LYSOPHOSPHOLIPID ACYLTRANSFERASE FROM THE MICROSOMES OF DEVELOPING SAFFLOWER SEEDS

Robert A. Moreau2 and Paul K. Stumpf

Department of Biochemistry and Biophysics, University of California, Davis, California 95616

Acyl-CoA:O-lysophospholipid acyltransferase activity was measured in extracts of developing safflower (Carthamus tinctorius var. UC-1) seeds. Acyltransferase activity was present in all subcellular fractions. The microsomal acyltransferase activity was solubilized with either 30 mM-n-octylglucoside, 1% deoxycholate, or 100 µM lysophosphatidylcholine. The pH optimum of the lysophosphatidylcholine-dependent acyltransferase activity was at 9.0. Among the various acyl-CoA's tested, oleoyl-CoA was the best substrate and with it the enzyme had a Km of 9.5 µM. Among the various acyl acceptors tested, lysophosphatidylcholine (oleoyl) gave the highest activity and the optimal concentration was 30 µM. Acyltransferase activity was stimulated by ethanol and inhibited by bovine serum albumin and divalent cations.

2 Present address: United States Department of Agriculture Plant Science Laboratory, 600 East Mermaid Lane, Wyndmoor, PA 19118.

1 Supported in part by the National Science Foundation, Grant No. PCM-7903976.






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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1982 by the American Society of Plant Biologists