The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus |
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| Affiliation: | 1. Istituto di Fisiologia Veterinaria e Biochimica, Università di Milano, Italy;2. Dipartimento di Genetica, Università di Pavia, Italy;3. Dipartimento di Chimica Organica, Università di Padova, Italy;4. CISMI, Centro Interuniversitario per lo Studio delle Macromolecole Informazionali, Italy;1. Department of Emergency Medicine, Yale University, New Haven, CT, USA;2. Department of Cardiology, Robert-Bosch-Krankenhaus, Stuttgart, Germany;3. Vita Salute University and San Raffaele Hospital, Milan, Italy;1. Department of Infectious Diseases, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;2. Institute of Molecular Virology (IMV), University of Muenster, Muenster 48149, Germany;3. Department of Computational Biology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;4. Department of Veterinary Pathology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;5. Department of Pediatrics, University of Tennessee Health Science Center, Memphis, TN 38163, USA;6. Children’s Foundation Research Institute, Le Bonheur Children’s Hospital, Memphis, TN 38103, USA |
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| Abstract: | The complete amino acid sequence of a basic (pI 9.0) fatty acid-binding protein purified from liver of Gallus domesticus was determined by automated Edman degradation of tryptic, CNBr/HFBA and Staphylococcus aureus protease peptides. The protein contains 125 amino acid residues which correspond to a molecular mass of 14094. The identification of the blocked N-terminus Ac-Ala required digestion of a SV-8 peptide with the acylamino acid-releasing enzyme prior to sequence analysis. Sequence comparison shows that chicken liver basic-FABP has a significant similarity to other proteins belonging to the superfamily of intracellular lipid molecule binding proteins. Moreover, these sequence data confirm that basic-FABP probably binds its substrate in a slightly different way when compared with other FABPs. Basic-FABP was submitted to the EMBL Data Library with an accession number of P80226 |
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