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Solubilisation of oleoyl‐CoA thioesterase, oleoyl‐CoA: phosphatidylcholine acyltransferase and oleoyl phosphatidylcholine desaturase
Author(s) -
Murphy Denis J.,
Woodrow Ian E.,
Latzko Erwin,
Mukherjee Kumar D.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80804-7
Subject(s) - thioesterase , phosphatidylcholine , acyltransferase , biochemistry , chemistry , digitonin , chromatography , microsome , enzyme , biosynthesis , phospholipid , membrane
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.