Characterization and amino acid sequence of a fatty acid-binding protein from human heart

摘要: The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation CNBr, BNPS-skatole [3'-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, digestion the with carboxypeptidase A. blocked N-terminal peptide citraconylated collisionally induced decomposition mass spectrometry. contains 132 residues, is enriched respect to threonine lysine, lacks cysteine, has an acetylated valine residue at N-terminus, Mr 14768 isoelectric point 5.25. This two short internal repeated sequences residues 48-54 114-119 located within regions predicted beta-structure decreasing hydrophobicity. These repeats are contained longer 48-60 114-125, which display 62% similarity. could accommodate charged uncharged moieties long-chain acids may represent domains consistent finding that binds 2 mol oleate or palmitate/mol protein. Detailed evidence for peptides been deposited as Supplementary Publication SUP 50143 (23 pages) British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., whom copies be obtained indicated in Biochem. J. (1988) 249, 5.