Bovine fatty acid binding proteins

摘要: When a 100000 ×g supernatant from bovine heart was incubated with [1-14C]oleic acid and subjected to isoelectric focusing, two fatty binding proteins (FABPs) points at 4.9 5.1 were detected. The purified on large scale first by heat precipitation of postmitochondrial supernatant, as well fractionation ammonium sulfate, then alternate application ion-exchange gel chromatography. The procedure afforded around 60 mg pure 1.5 kg fresh muscle. Relative molecular masses 15 300 ± 1600 for both derived sodium dodecyl sulfate/polyacrylamide electrophoresis, chromatography, sedimentation velocity amino analysis. Up 50% the proteins' secondary structures consisted β-sheet. N-termini peptide chains blocked; compositions similar, but differed considerably those FABPs isolated liver [Haunerland et al. (1984) Hoppe Seyler's Z. Physiol. Chem. 365, 365–376]. Whereas hepatic changed their pI upon acids, cardiac did not. Cardiac immunologically identical, not cross-react proteins. A reversible, concentration-dependent self-association reported FABP pig [Fournier (1983) Biochemistry 22, 1863–1872] observed heart. Changes concentration alter structure, intrinsic fluorescence or coefficient protein.