Diacylglycerol acyltransferase in maturing sunflower seeds

descriptionPublicationkeyboard_double_arrow_right Article 01 Dec 2000 English Publisher:Portland Press Ltd.Journal:Biochemical Society Transactions, volume 28, pages 689-692 (issn: 0300-5127, eissn: 1470-8752,

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Authors: S, Triki; J, Ben Hamida; P, Mazliak;

doi: 10.1042/bst0280689 , 10.1042/0300-5127:0280689

pmid: 11171172

Diacylglycerol acyltransferase in maturing sunflower seeds

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Abstract

Developing sunflower seeds exhibit a high diacylglycerol acyltransferase (DAGAT, EC 2.3.1.20) activity. The distribution of the enzyme has been studied in subcellular fractions prepared by differential centrifugation of seed homogenate. Its activity was characterized using [1-14C]oleoyl-CoA and diolein dispersed in Tween 20. Some properties of the microsomal fraction of DAGAT were investigated. Hyperbolic kinetics were observed, the apparent Km was 60 μM and the specific activity of the reaction 15 pmol/min/mg of protein. Addition of BSA (0.1%) stimulated oleate incorporation, which was not dependent on the presence of exogenous diacylglycerol. Detergents which might solubilize DAGAT, Triton X-100 and CHAPS, were tested for enzyme inhibition, and CHAPS was found to be the least denaturing.

Related Organizations

Laboratoire de Physiologie Cérébrale
France

Keywords

Protein Denaturation, Octoxynol, Detergents, Cholic Acids, Diglycerides, Kinetics, Seeds, Helianthus, Acyl Coenzyme A, Carbon Radioisotopes, Diacylglycerol O-Acyltransferase, Acyltransferases

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