Purification of high affinity fatty acid receptors in rat myocardial sarcolemmal membranes.
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.
D000818:Animals; D005227:Fatty Acids / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D009206:Myocardium / Q000378:metabolism*; D051381:Rats; D012508:Sarcolemma / Q000378:metabolism*; D013816:Thermodynamics
D005227:Fatty Acids