Solubilisation of oleoyl-CoA thioesterase, oleoyl-CoA: phosphatidylcholine acyltransferase and oleoyl phosphatidylcholine desaturase. The oleate desaturase system of pea leaf microsomes

Abstract

Membrane-bound enzymes involved in oleate metabolism in microsomes from pea (Pisum sativum L.) leaves were solubilised using detergents, such as n-octyl glucoside, Triton X-100, digitonin or cholate. The detergents were found to be inhibitory to oleoyl-CoA thioesterase, oleoyl-CoA:phosphatidylcholine acyltransferase and oleoyl phosphatidylcholine desaturase. Detergent removal by dialysis resulted in the restoration of activity of both the solubilised oleoyl-CoA thioesterase and oleoyl-CoA:phosphatidylcholine acyltransferase. The putative components of the oleoyl phosphatidylcholine desaturase system were also partially solubilised. © 1983.