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Diffication of high affinity fatty acid receptors in rat myocardial sarcolemmal membranes
Author(s) -
Fujii Satoshi,
Kawaguchi Hideaki,
Yasuda Hisakazu
Publication year - 1987
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02540374
Subject(s) - chromatography , chemistry , membrane , affinity chromatography , dissociation constant , size exclusion chromatography , fatty acid binding protein , biochemistry , receptor , affinity electrophoresis , homogeneous , polyacrylamide gel electrophoresis , clinical chemistry , fatty acid , enzyme , physics , gene , thermodynamics
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.