RGD Reference Report - Purification and characterization of fatty-acid-binding proteins from rat heart and liver. - Rat Genome Database

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Purification and characterization of fatty-acid-binding proteins from rat heart and liver.

Authors: Glatz, JF  Janssen, AM  Baerwaldt, CC  Veerkamp, JH 
Citation: Glatz JF, etal., Biochim Biophys Acta. 1985 Oct 23;837(1):57-66.
RGD ID: 1582415
Pubmed: PMID:4052437   (View Abstract at PubMed)

Fatty-acid-binding proteins were purified from delipidated cytosols of rat heart and liver by gel filtration and anion-exchange chromatography at pH 8.0 and by repeated gel filtration, respectively. Homogeneity of both proteins was demonstrated by a single band on polyacrylamide gels; each had a molecular weight of about 14 000. Liver fatty-acid-binding protein is more basic (pI, 8.1) than that of heart (pI, 7.0) and contains more basic amino acids. Examination of fatty acid binding by the binding proteins from heart and liver revealed the presence of a single class of fatty-acid-binding sites in both cases with an apparent dissociation constant for palmitate of about 1 microM. Liver fatty- acid-binding protein shows similar binding characteristics for palmitate, oleate and arachidonate. Palmitate bound to heart fatty- acid-binding protein was a good substrate for oxidation by rat heart mitochondria. The results show that the fatty-acid-binding proteins from rat heart and liver are closely related, but that they are distinct proteins.

Objects referenced in this article
Gene Fabp3 fatty acid binding protein 3 Rattus norvegicus

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