Solubilisation of oleoyl‐CoA thioesterase, oleoyl‐CoA: phosphatidylcholine acyltransferase and oleoyl phosphatidylcholine desaturase

FEBS Letters

Woodrow, Ian E.²  Murphy, Denis J.²  Latzko, Erwin²  Mukherjee, Kumar D.¹ 

[1] Bundesanstalt für Fettforschung, Piusallee 68/76, D-4400 Münster, FRG;Botanisches Institut der Universität Münster, Schloßgarten 3, D-4400 Münster, FRG

关键词: Microsome;    Oleoyl-CoA thioesterase;    Oleoyl-CoA:phosphatidylcholine acyltransferase;    Oleoyl phosphatidylcholine desaturase;    CoA;    coenzyme A;    PC;    phosphatidylcholines;    FA;    unesterified fatty acids;    18:1;    oleoyl moieties;    18:2;    linoleoyl moieties;   

DOI  :  10.1016/0014-5793(83)80804-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown