The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus
| Autor: | Severino Ronchi, Ludovica Faotto, Paola Spadon, Fabrizio Ceciliani, Hugo L. Monaco |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Physiology
Sequence analysis medicine.medical_treatment Molecular Sequence Data Peptide Biology Alkalies Fatty Acid-Binding Proteins Myelin P2 Protein Biochemistry Fatty acid-binding protein medicine Animals Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Protease Molecular mass Edman degradation Protein primary structure General Medicine Molecular biology Neoplasm Proteins chemistry Liver lipids (amino acids peptides and proteins) Carrier Proteins Chickens |
| Zdroj: | Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 109(2-3) |
| ISSN: | 1096-4959 |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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