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Article: Timed photoaffinity labeling and characterization of bile acid binding and transport proteins in rat ileum

TitleTimed photoaffinity labeling and characterization of bile acid binding and transport proteins in rat ileum
Authors
Issue Date1993
PublisherAmerican Physiological Society. The Journal's web site is located at http://ajpcon.physiology.org/
Citation
American Journal Of Physiology - Gastrointestinal And Liver Physiology, 1993, v. 265 n. 1 28-1, p. G56-G62 How to Cite?
AbstractRat ileal enterocytes were radiolabeled by flash photolysis with a photolabile derivative of taurocholate (7,7-azo-[3H]TC) and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Maximal labeling of the bile acid binding proteins (BABPs) was achieved between 15 and 90 s. When enterocytes were pulsed with 7,7-azo-[3H]TC for 2 min, and then 0.5 mM TC was added to chase the radiolabel, the radioactivity in the BABPs was displaced by 50% after 2 min. The 99-kDa brush-border membrane (BBM) protein had the highest initial labeling rate, followed by 43-kDa actin, 35- and 14- kDa cytosolic proteins, 54-kDa basolateral membrane (BLM) protein, 59-kDa BLM-associated protein, and 20-kDa microsomal protein. When a mixed microsomal and cytosolic fraction was photolabeled with 7,7-azo-[3H]TC and then separated, the 20-kDa microsomal protein was labeled. However, if the microsomal fraction alone was photolabeled, the 20-kDa protein was not labeled, suggesting this protein required a cytosolic cofactor for labeling. Using Triton X-114 phase separation and EDTA extraction, the BABPs were separated into amphiphilic integral membrane proteins (99- and 54-kDa proteins) and hydrophilic proteins (14-, 35-, 43-, and 59-kDa proteins). From these data, a model is proposed for transcellular bile acid transport in rat ileal enterocytes.
Persistent Identifierhttp://hdl.handle.net/10722/167506
ISSN
1998 Impact Factor: 3.077
2004 SCImago Journal Rankings: 1.102
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorMullady, Een_US
dc.contributor.authorWilson, FAen_US
dc.date.accessioned2012-10-08T03:07:50Z-
dc.date.available2012-10-08T03:07:50Z-
dc.date.issued1993en_US
dc.identifier.citationAmerican Journal Of Physiology - Gastrointestinal And Liver Physiology, 1993, v. 265 n. 1 28-1, p. G56-G62en_US
dc.identifier.issn0002-9513en_US
dc.identifier.urihttp://hdl.handle.net/10722/167506-
dc.description.abstractRat ileal enterocytes were radiolabeled by flash photolysis with a photolabile derivative of taurocholate (7,7-azo-[3H]TC) and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Maximal labeling of the bile acid binding proteins (BABPs) was achieved between 15 and 90 s. When enterocytes were pulsed with 7,7-azo-[3H]TC for 2 min, and then 0.5 mM TC was added to chase the radiolabel, the radioactivity in the BABPs was displaced by 50% after 2 min. The 99-kDa brush-border membrane (BBM) protein had the highest initial labeling rate, followed by 43-kDa actin, 35- and 14- kDa cytosolic proteins, 54-kDa basolateral membrane (BLM) protein, 59-kDa BLM-associated protein, and 20-kDa microsomal protein. When a mixed microsomal and cytosolic fraction was photolabeled with 7,7-azo-[3H]TC and then separated, the 20-kDa microsomal protein was labeled. However, if the microsomal fraction alone was photolabeled, the 20-kDa protein was not labeled, suggesting this protein required a cytosolic cofactor for labeling. Using Triton X-114 phase separation and EDTA extraction, the BABPs were separated into amphiphilic integral membrane proteins (99- and 54-kDa proteins) and hydrophilic proteins (14-, 35-, 43-, and 59-kDa proteins). From these data, a model is proposed for transcellular bile acid transport in rat ileal enterocytes.en_US
dc.languageengen_US
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://ajpcon.physiology.org/en_US
dc.relation.ispartofAmerican Journal of Physiology - Gastrointestinal and Liver Physiologyen_US
dc.subject.meshAffinity Labelsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAzo Compoundsen_US
dc.subject.meshBile Acids And Salts - Metabolismen_US
dc.subject.meshCarrier Proteins - Metabolismen_US
dc.subject.meshCytosol - Metabolismen_US
dc.subject.meshEdetic Aciden_US
dc.subject.meshHydroxysteroid Dehydrogenasesen_US
dc.subject.meshIleum - Cytology - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMicrosomes - Metabolismen_US
dc.subject.meshPolyethylene Glycolsen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Sprague-Dawleyen_US
dc.subject.meshTime Factorsen_US
dc.titleTimed photoaffinity labeling and characterization of bile acid binding and transport proteins in rat ileumen_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.pmid8338173-
dc.identifier.scopuseid_2-s2.0-0027328995en_US
dc.identifier.volume265en_US
dc.identifier.issue1 28-1en_US
dc.identifier.spageG56en_US
dc.identifier.epageG62en_US
dc.identifier.isiWOS:A1993LP43100071-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridMullady, E=6506654737en_US
dc.identifier.scopusauthoridWilson, FA=7202849433en_US

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