Purification and properties of fatty acid synthetase from a human breast cell line.
A human mammary epithelial cell line (SKBr3) has been identified in which fatty acid synthetase constitutes up to 28%, by weight of the cytosolic proteins. The enzymes has been purified to near homogeneity from this cell line and some of its properties studied. In common with fatty acid synthetases from other animal tissues, the enzyme is a 480 000 dalton dimer of similar molecular weight subunits, it synthesizes predominantly palmitic acid and is inactive in the absence of free coenzyme A. The kinetic properties and amino acid composition of the enzyme are also similar to those of fatty acid synthetases from various tissues of other animals. Appreciable structural resemblance between human and rodent fatty acid synthetases is indicated by studies on the immunological cross-reactivities of these enzymes.
D000596:Amino Acids / Q000032:analysis; D001940:Breast / Q000201:enzymology*; D002460:Cell Line; D003065:Coenzyme A / Q000378:metabolism; D003429:Cross Reactions; D004848:Epithelium / Q000201:enzymology; D064429:Fatty Acid Synthases / Q000302:isolation & purification*; D005260:Female; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000096:biosynthesis
D000596:Amino Acids; D046911:Macromolecular Substances; D010169:Palmitic Acids; D019308:Palmitic Acid; D064429:Fatty Acid Synthases; D003065:Coenzyme A