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Abstract
We have isolated in pure form a fatty acid binding protein (FABP) from human cardiac muscle. After preparation of a 100,000 g supernatant fraction, the procedure required only one gel chromatographic (Sephacryl S 200) and two cation exchange (CM-Sephadex C 50) steps. The recovery of FABP was 55%. Pure FABP (12.5 mg) was obtained from a 1-g of dry powder equivalent of the high-speed supernatant. The protein had an Mr of 15,500 +/- 1,000 Da and an isoelectric point of 5.3. The properties of human cardiac FABP, i.e., molecular mass, isoelectric point, amino acid composition, ultraviolet spectrum, and affinities for hydrophobic ligands, were close to those found for FABPs from bovine heart (Jagschies et al. 1985. Eur. J. Biochem. 152: 537-545). In addition, immunological cross-reactivities showed a relationship between FABPs from several mammalian heart tissues. The data elaborated by us and others support the existence of a cardiac-type FABP that is distinct from the well-defined hepatic-type and gut-type FABPs.
Highlights
In the course of our studies on intracellular transport and recognition of fatty acids [22, 24,25,26], we present here an expeditious four-step procedure for the isolation of fatty acid binding protein (FABP) from human heart that affords mg amounts of pure protein
The bands' superposition reveals the presence of a fatty acid binding protein, whose affinity for oleic acid was strong enough not to dissociate under the electric field applied
To avoid initial losses of FABP during bulk fractionation with ammonium sulfate [22], we started with a supernatant prepared by high-speed ultracentrifugation
Summary
Pure FABP (12.5 mg) was obtained from a 1-g of dry powder equivalent of the high-speed supernatant. The protein had an M,of 15,500 & 1,000Da and an isoelectric point of 5.3. The properties of human cardiac FABP, i.e., molecular mass, isoelectric point, amino acid composition, ultraviolet spectrum, and affinitiesfor hydrophobic ligands,were close to those found for FABPs from bovine heart Immunological cross-reactivities showed a relationship between FABPs from several mammalian heart tissues.l The data elaborated by us and others support the existence of a cardiac-type FABP that is distinct from the well-defined hepatic-type and gut-type FABPs.-Unterberg, C., C. Isolation and characterizationof the fatty acid binding protein from human heart.
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