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Article: Characterization of a novel 14 kDa bile acid-binding protein from rat ileal cytosol

TitleCharacterization of a novel 14 kDa bile acid-binding protein from rat ileal cytosol
Authors
Issue Date1991
Citation
Biochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1991, v. 1078 n. 3, p. 329-335 How to Cite?
AbstractA 14 kDa polypeptide in rat ileal cytosol has been identified as the major intestinal cytosolic bile acid-binding protein (I-BABP) by photoaffinity labeling with the radiolabeled 7,7-azo derivative of taurocholate (7,7-azo-TC). To further characterize I-BABP, the protein was purified by lysylglycocholate Sepharose 4B affinity and DE-52 anion-exchange chromatography. The purified I-BABP contained a single 14 kDa band on SDS-PAGE. The 14 kDa protein showed a 26-fold increase in binding affinity for [ 3H]7,7-azo-TC compared to cytosolic protein. Immunoblotting of protein fractions separated by affinity chromatography showed that neither liver fatty acid binding protein (L-FABP) nor intestinal fatty acid binding protein (I-FABP) bind to the affinity column and that the 14 kDa protein which bound to the column and was subsequently eluted with detergent did not cross-react with anti-L-FABP or anti-I-FABP. The 14 kDa protein labeled with [ 3H]7,7-azo-TC was radioimmunoprecipitated from cytosol by rabbit antiserum raised against purified I-BABP. I-BABP was shown to have a blocked N-terminus; however, its mixed internal sequence generated from cyanogen bromide-cleaved protein and amino acid composition indicated that it was related to (although clearly distinct from) both I-FABP and L-FABP. These studies have isolated a 14 kDa bile acid-binding protein from rat ileal cytosol which is immunologically and biochemically distinct from I-FABP and L-FABP.
Persistent Identifierhttp://hdl.handle.net/10722/167498
ISSN
2004 Impact Factor: 3.079
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorGong, Yen_US
dc.contributor.authorGeoghegan, KFen_US
dc.contributor.authorWilson, FAen_US
dc.date.accessioned2012-10-08T03:07:43Z-
dc.date.available2012-10-08T03:07:43Z-
dc.date.issued1991en_US
dc.identifier.citationBiochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1991, v. 1078 n. 3, p. 329-335en_US
dc.identifier.issn0167-4838en_US
dc.identifier.urihttp://hdl.handle.net/10722/167498-
dc.description.abstractA 14 kDa polypeptide in rat ileal cytosol has been identified as the major intestinal cytosolic bile acid-binding protein (I-BABP) by photoaffinity labeling with the radiolabeled 7,7-azo derivative of taurocholate (7,7-azo-TC). To further characterize I-BABP, the protein was purified by lysylglycocholate Sepharose 4B affinity and DE-52 anion-exchange chromatography. The purified I-BABP contained a single 14 kDa band on SDS-PAGE. The 14 kDa protein showed a 26-fold increase in binding affinity for [ 3H]7,7-azo-TC compared to cytosolic protein. Immunoblotting of protein fractions separated by affinity chromatography showed that neither liver fatty acid binding protein (L-FABP) nor intestinal fatty acid binding protein (I-FABP) bind to the affinity column and that the 14 kDa protein which bound to the column and was subsequently eluted with detergent did not cross-react with anti-L-FABP or anti-I-FABP. The 14 kDa protein labeled with [ 3H]7,7-azo-TC was radioimmunoprecipitated from cytosol by rabbit antiserum raised against purified I-BABP. I-BABP was shown to have a blocked N-terminus; however, its mixed internal sequence generated from cyanogen bromide-cleaved protein and amino acid composition indicated that it was related to (although clearly distinct from) both I-FABP and L-FABP. These studies have isolated a 14 kDa bile acid-binding protein from rat ileal cytosol which is immunologically and biochemically distinct from I-FABP and L-FABP.en_US
dc.languageengen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBile Acids And Salts - Metabolismen_US
dc.subject.meshCarrier Proteins - Isolation & Purificationen_US
dc.subject.meshChromatography, Ion Exchangeen_US
dc.subject.meshCytosol - Chemistryen_US
dc.subject.meshHydroxysteroid Dehydrogenasesen_US
dc.subject.meshIleum - Chemistryen_US
dc.subject.meshImmunoblottingen_US
dc.subject.meshMaleen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.titleCharacterization of a novel 14 kDa bile acid-binding protein from rat ileal cytosolen_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0167-4838(91)90152-Pen_US
dc.identifier.pmid1859823-
dc.identifier.scopuseid_2-s2.0-0025894881en_US
dc.identifier.volume1078en_US
dc.identifier.issue3en_US
dc.identifier.spage329en_US
dc.identifier.epage335en_US
dc.identifier.isiWOS:A1991FY97800005-
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridGong, Y=7402475196en_US
dc.identifier.scopusauthoridGeoghegan, KF=7004009236en_US
dc.identifier.scopusauthoridWilson, FA=7202849433en_US

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