Diffication of high affinity fatty acid receptors in rat myocardial sarcolemmal membranes

Abstract
High affinity receptors for fatty acid were purified from rat cardiac sarcolemmal membrane using gel filtration, DEAE-cellulose chromatography and affinity chromatography. The purified protein was homogeneous on polyacrylamide gel electrophoresis with the molecular weight of 60 kDa. Binding studies revealed the presence of a single class of high affinity binding sites with an apparent dissociation constant of 1.0 μM and a maximal binding capacity of 12.1 pmol/μg protein.