Isolation and characterization of the fatty acid binding protein from human heart.
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.
D000596:Amino Acids / Q000032:analysis; D002352:Carrier Proteins / Q000302:isolation & purification*; D003429:Cross Reactions; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D006801:Humans; D005779:Immunodiffusion; D007526:Isoelectric Point; D008970:Molecular Weight; D009206:Myocardium / Q000032:analysis*; D009363:Neoplasm Proteins; D013056:Spectrophotometry, Ultraviolet; D025521:Tumor Suppressor Proteins
D000596:Amino Acids; D002352:Carrier Proteins; C107608:FABP7 protein, human; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D025521:Tumor Suppressor Proteins