The 14 kDa bile acid binding protein of rat ileal cytosol (I-BABP), previously shown to be the major intracellular transporter of bile acids in enterocytes, was purified by affinity chromatography and gel electrophoresis. Enzymatic digestion of I-BABP which had been electroblotted to nitrocellulose led to the recovery and sequence analysis of four peptides representing 47 residues of sequence (approximately 35% of the full sequence). All the peptide sequences displayed high levels of identity (greater than 60%) and homology (greater than 80%) to the sequences of porcine and canine gastrotropin. This high level of homology together with other features of I-BABP identify it as rat gastrotropin, establishing gastrotropin as the major intracellular bile acid carrier of rat enterocytes.
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| rdf:type | |
| rdfs:comment |
The 14 kDa bile acid binding protein of rat ileal cytosol (I-BABP), previously shown to be the major intracellular transporter of bile acids in enterocytes, was purified by affinity chromatography and gel electrophoresis. Enzymatic digestion of I-BABP which had been electroblotted to nitrocellulose led to the recovery and sequence analysis of four peptides representing 47 residues of sequence (approximately 35% of the full sequence). All the peptide sequences displayed high levels of identity (greater than 60%) and homology (greater than 80%) to the sequences of porcine and canine gastrotropin. This high level of homology together with other features of I-BABP identify it as rat gastrotropin, establishing gastrotropin as the major intracellular bile acid carrier of rat enterocytes.
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| skos:exactMatch | |
| uniprot:name |
Biochem. Biophys. Res. Commun.
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| uniprot:author |
Geoghegan K.F.,
Gong Y.-Z.,
Lanzetti A.J.,
Lin M.C.,
Vodenlich A.D. Jr.,
Wilson F.A.
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| uniprot:date |
1991
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| uniprot:pages |
1147-1154
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| uniprot:title |
Identification of the 14 kDa bile acid transport protein of rat ileal cytosol as gastrotropin.
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| uniprot:volume |
177
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| dc-term:identifier |
doi:10.1016/0006-291X(91)90659-U
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