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- Scopus: eid_2-s2.0-0027328995
- PMID: 8338173
- WOS: WOS:A1993LP43100071
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Article: Timed photoaffinity labeling and characterization of bile acid binding and transport proteins in rat ileum
Title | Timed photoaffinity labeling and characterization of bile acid binding and transport proteins in rat ileum |
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Authors | |
Keywords | bile acid binding proteins photoaffinity labeling rat ileal enterocytes taurocholate |
Issue Date | 1993 |
Publisher | American 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? |
Abstract | Rat 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 Identifier | http://hdl.handle.net/10722/167506 |
ISSN | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Lin, MC | en_US |
dc.contributor.author | Mullady, E | en_US |
dc.contributor.author | Wilson, FA | en_US |
dc.date.accessioned | 2012-10-08T03:07:50Z | - |
dc.date.available | 2012-10-08T03:07:50Z | - |
dc.date.issued | 1993 | en_US |
dc.identifier.citation | American Journal Of Physiology - Gastrointestinal And Liver Physiology, 1993, v. 265 n. 1 28-1, p. G56-G62 | en_US |
dc.identifier.issn | 0002-9513 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167506 | - |
dc.description.abstract | Rat 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.language | eng | en_US |
dc.publisher | American Physiological Society. The Journal's web site is located at http://ajpcon.physiology.org/ | en_US |
dc.relation.ispartof | American Journal of Physiology - Gastrointestinal and Liver Physiology | en_US |
dc.subject | bile acid binding proteins | - |
dc.subject | photoaffinity labeling | - |
dc.subject | rat ileal enterocytes | - |
dc.subject | taurocholate | - |
dc.subject.mesh | Affinity Labels | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Azo Compounds | en_US |
dc.subject.mesh | Bile Acids And Salts - Metabolism | en_US |
dc.subject.mesh | Carrier Proteins - Metabolism | en_US |
dc.subject.mesh | Cytosol - Metabolism | en_US |
dc.subject.mesh | Edetic Acid | en_US |
dc.subject.mesh | Hydroxysteroid Dehydrogenases | en_US |
dc.subject.mesh | Ileum - Cytology - Metabolism | en_US |
dc.subject.mesh | Male | en_US |
dc.subject.mesh | Membrane Glycoproteins | en_US |
dc.subject.mesh | Microsomes - Metabolism | en_US |
dc.subject.mesh | Polyethylene Glycols | en_US |
dc.subject.mesh | Rats | en_US |
dc.subject.mesh | Rats, Sprague-Dawley | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.title | Timed photoaffinity labeling and characterization of bile acid binding and transport proteins in rat ileum | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lin, MC:mcllin@hkucc.hku.hk | en_US |
dc.identifier.authority | Lin, MC=rp00746 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.pmid | 8338173 | - |
dc.identifier.scopus | eid_2-s2.0-0027328995 | en_US |
dc.identifier.volume | 265 | en_US |
dc.identifier.issue | 1 28-1 | en_US |
dc.identifier.spage | G56 | en_US |
dc.identifier.epage | G62 | en_US |
dc.identifier.isi | WOS:A1993LP43100071 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Lin, MC=7404816359 | en_US |
dc.identifier.scopusauthorid | Mullady, E=6506654737 | en_US |
dc.identifier.scopusauthorid | Wilson, FA=7202849433 | en_US |
dc.identifier.issnl | 0002-9513 | - |