Isolation of an acyl carrier protein component from the multienzyme complex of yeast fatty acid synthetase

[14C]Pantetheine fatty acid synthetase from baker's yeast was denatured in guanidine hydrochloride. Then the protein components of the multienzyme complex were subjected to a Sephadex filtration in guanidine hydrochloride and a preparative polyacrylamide gel electrophoresis in a phenol containing medium. It could be demonstrated that the [14C]pantetheine label was co-valently bound to one of the smallest polypeptide chains of the multienzyme complex. In analogy to the soluble acyl carrier protein which was first isolated from Escherichia coli and contained 4′-phosphopantetheine as a prosthetic group, the pantetheine-protein component of the yeast multienzyme complex was denoted as yeast acyl carrier protein. Its molecular weight seemed to be higher and its amino acid composition different from the E. coli acyl carrier protein.