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. 1987 Jul;22(7):544-6.
doi: 10.1007/BF02540374.

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

S Fujii, H Kawaguchi, H Yasuda

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

S Fujii et al. Lipids. 1987 Jul.

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 microM and a maximal binding capacity of 12.1 pmol/micrograms protein.

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