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

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Lipids

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.

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Abbreviations

FABP:

fatty acid binding protein

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Authors and Affiliations

  1. Department of Cardiovascular Medicine, Hokkaido University School of Medicine, Sapporo, Japan

    Satoshi fujii, Hideaki Kawaguchi & Hisakazu Yasuda

Authors
  1. Satoshi fujii
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  2. Hideaki Kawaguchi
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  3. Hisakazu Yasuda
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fujii, S., Kawaguchi, H. & Yasuda, H. Diffication of high affinity fatty acid receptors in rat myocardial sarcolemmal membranes. Lipids 22, 544–546 (1987). https://doi.org/10.1007/BF02540374

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  • DOI: https://doi.org/10.1007/BF02540374

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