Isolation of thioesterase and acyl carrier protein activities liberated by elastase digestion of pigeon liver fatty acid synthetase |
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Authors: | R N Puri J W Porter |
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Institution: | 1. Lipid Metabolism Laboratory William S. Middleton Memorial Veterans Hospital Madison, Wisconsin 53706 USA;2. the Department of Physiological Chemistry University of Wisconsin Madison, Wisconsin 53706 USA |
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Abstract: | Proteolysis of pigeon liver fatty acid synthetase with elastase cleaves the thioesterase component and an acyl carrier protein-containing peptide from the multienzyme complex. These proteins are then separated in one step by gel filtration on a Sephadex G-75 column. Each of the eluted proteins is homogeneous, as determined by polyacrylamide gel electrophoresis. The molecular weight of each has been estimated to be 36,000 and 12,000 daltons, respectively. |
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