Purification and characterization of the fatty acid synthase from Bugula neritina

The fatty acid synthase from Bugula neritina has been purified 100-fold usi ng ammonium sulfate precipitation, ion-exchange and size exclusion chromato graphy. The purified enzyme has a molecular weight of approximately 382 000 Da, as judged by gel filtration. Polyacrylamide gel electrophoresis under denaturing conditions in the presence of SDS revealed one major protein ban d of approximately 190 000 Da suggesting that the enzyme is a homodimer. Th e size of the enzyme, together with the observation that the FAS activity i s independent of the concentration of acyl carrier protein, indicate that t he FAS from Bugula neritina is a type I. A detailed analysis of the product s of the purified FAS indicated that palmitic acid is the primary product a nd longer chain fatty acids are not produced. (C) 2001 Elsevier Science Inc . All rights reserved.