Fabrizio Ceciliani , Hugo L. Monaco , Severino Ronchi , Ludovica Faotto , Paola Spadon
{"title":"The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus","authors":"Fabrizio Ceciliani , Hugo L. Monaco , Severino Ronchi , Ludovica Faotto , Paola Spadon","doi":"10.1016/0305-0491(94)90010-8","DOIUrl":null,"url":null,"abstract":"<div><p>The complete amino acid sequence of a basic (pI 9.0) fatty acid-binding protein purified from liver of <em>Gallus domesticus</em> was determined by automated Edman degradation of tryptic, CNBr/HFBA and <em>Staphylococcus aureus</em> protease peptides. The protein contains 125 amino acid residues which correspond to a molecular mass of 14094. The identification of the blocked <em>N</em>-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</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 261-271"},"PeriodicalIF":0.0000,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90010-8","citationCount":"38","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0305049194900108","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 38
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