Rat heart fatty acid-binding protein is highly homologous to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin.

摘要: The rat heart contains an abundant cytosolic protein which binds long chain fatty acids. We have determined its primary structure by Edman degradation of peptides generated from chymotryptic, tryptic, and elastase digestions. This polypeptide (Mr = 14,992) 134 amino acids has a blocked (acetylated) NH2 terminus. sequence acid-binding (FABP) is remarkably similar to the murine adipocyte 422 P2 peripheral nerve myelin. Computer-assisted alignment FABP revealed that 82 132 comparable residues are identical (62%). There 77 identities out 131 possible matches between this human myelin (59%). Similar comparisons demonstrate significant homology several other proteins bind hydrophobic ligands. rank order similarity is: greater than cellular retinoic retinol-binding II intestinal liver FABP. These eight sequences form family paralogous homologues. Heart region internal involving tandemly arrayed oligopeptides spanning 71-100 101-131. feature not found in sequences. endogenous ligands bound 422, P2, been defined. Interpretation biological significance their structural similarities differences will require information about ligand specificities affinities.