The isolation of acyl carrier protein from the pigeon liver fatty acid synthetase complex1 II |
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Authors: | A A Qureshi F A Lornitzo J W Porter |
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Affiliation: | Lipid Metabolism Laboratory, Veterans Administration Hospital, and the Department of Physiological Chemistry, University of Wisconsin Madison, Wisconsin 53706 USA |
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Abstract: | A low molecular weight protein of less than 10, 000 Daltons has been isolated from Subunit I (β-ketoacyl thioester reductase) of the pigeon liver fatty acid synthetase complex and purified to homogeneity. This protein contains all of the [14C]-labeled pantetheine incorporated into the fatty acid synthetase on injection of [14C]-labeled pantetheine into pigeons. It also has one β-alanine and one sulfhydryl group. This protein is an acceptor of an acetyl group from acetyl-CoA and a malonyl group from malonyl-CoA in the presence of Subunit II (transacylase). In these respects it is very similar to acyl carrier protein. |
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