1887

Abstract

Fractionated extracts of were found to contain the readily dissociable type of fatty acid synthase complex. For optimal activity the partially purified synthase required the presence of acetyl-CoA, malonyl-CoA, NADH and NADPH as well as a cell-free fraction containing the acyl carrier protein (ACP). When ACP-containing fractions obtained from grown in the presence of [1-C]pantothenate were subjected to sodium dodecyl sulphate-polyacrylamide gel electrophoresis, the radioactivity was located in a peak corresponding to a molecular weight of approx. 8500-9000. The biological activity of the ACP was relatively heat-stable and trypsin-resistant. When the labelled ACP-containing fraction was subjected to gel filtration on a calibrated Sephadex G-75 column, a radioactive peak corresponding to a molecular weight of 22000 was obtained that could participate in the CO-malonyl-CoA exchange reaction in the presence of the other requisite components.

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/content/journal/micro/10.1099/00221287-127-1-121
1981-11-01
2019-10-21
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