Purification and characterization of the fatty acid ...

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Title Purification and characterization of the fatty acid synthase from Bugula neritina
Author(s) J. Wen, Russell G. Kerr
Journal Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
Date 2001
Volume 128
Issue 3
Start page 445
End page 450
Abstract The fatty acid synthase from Bugula neritina has been purified 100-fold using ammonium sulfate precipitation, ion-exchange and size exclusion chromatography. 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 band of approximately 190,000 Da suggesting that the enzyme is a homodimer. The size of the enzyme, together with the observation that the FAS activity is independent of the concentration of acyl carrier protein, indicate that the FAS from Bugula neritina is a type I. A detailed analysis of the products of the purified FAS indicated that palmitic acid is the primary product and longer chain fatty acids are not produced.
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