FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1976173696> ?p ?o ?g. }

• W1976173696 endingPage "1282" @default.
• W1976173696 startingPage "1279" @default.
• W1976173696 abstract "Sodium-dependent bile acid transport is a well-established function of the sinusoidal segment of the hepatocyte plasma membrane. Evidence has been provided previously by the authors for the existence of a putative sinusoidal plasma membrane sodium-dependent bile acid transporter with a mass of 49 kD. This protein has been partially characterized with a monoclonal antibody and by reconstitution in proteoliposomes. Further characterization is provided in the paper under discussion. The transporter was isolated from plasma membranes and from endoplasmic reticulum by immunoprecipitation with a monoclonal antibody. The protein was separated from antibody by means of HPLC and SDS-PAGE with electroelution. Amino acid analysis and NH2-terminal amino acid sequencing were performed. For both preparations, it was shown that the NH2-terminal amino acid sequence was identical, and the amino acid composition was similar to results obtained for the microsomal enzyme epoxide hydrolase. Purified mEH was immunoprecipitated with the monoclonal antibody which precipitated the plasma membrane protein. Isoelectric focusing established that the isoelectric points for epoxide hydrolase and the proteins isolated from the endoplasmic reticulum and plasma membranes were identical. The peptide maps prepared by subjecting the three proteins to enzymatic fragmentation with subtilisin were essentially identical. Because of the known contamination of plasma membrane fractions with endoplasmic reticulum and because of the high specific activity of epoxide hydrolase in endoplasmic reticulum, special attention was devoted to the question of the localization of the enzyme/transporter in plasma membrane. It was possible to show that virtually all of the immunoprecipitated protein obtained from intact cells derived from plasma membrane and that only a small fraction could be explained as having originated in endoplasmic reticulum. Finally, a hydrophobic plot of the amino acid sequence of epoxide hydrolase suggested that the protein contained four potential transmembrane domains. It could be concluded that a/the 49-kD sinusoidal plasma membrane sodium-dependent bile acid transporter protein was closely similar or identical to epoxide hydrolase. In view of the relatively small mass of the protein and its limited number of potential transmembrane domains, it appeared probable that the physiological membrane transporter consists of an assembly of 49-kD monomers or an assembly of heterologous proteins including the 49-kD protein." @default.
• W1976173696 created "2016-06-24" @default.
• W1976173696 creator A5019271587 @default.
• W1976173696 creator A5085958014 @default.
• W1976173696 date "1993-11-01" @default.
• W1976173696 modified "2023-09-26" @default.
• W1976173696 title "True transport: One or more sodium-dependent bile acid transporters?" @default.
• W1976173696 cites W1011303884 @default.
• W1976173696 cites W1481602754 @default.
• W1976173696 cites W1501455003 @default.
• W1976173696 cites W1519480067 @default.
• W1976173696 cites W1554692773 @default.
• W1976173696 cites W1560826405 @default.
• W1976173696 cites W1603127702 @default.
• W1976173696 cites W1993689132 @default.
• W1976173696 cites W2031847842 @default.
• W1976173696 cites W2041562911 @default.
• W1976173696 cites W2045875385 @default.
• W1976173696 cites W4302766139 @default.
• W1976173696 doi "https://doi.org/10.1002/hep.1840180539" @default.
• W1976173696 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8225237" @default.
• W1976173696 hasPublicationYear "1993" @default.
• W1976173696 type Work @default.
• W1976173696 sameAs 1976173696 @default.
• W1976173696 citedByCount "4" @default.
• W1976173696 countsByYear W19761736962013 @default.
• W1976173696 crossrefType "journal-article" @default.
• W1976173696 hasAuthorship W1976173696A5019271587 @default.
• W1976173696 hasAuthorship W1976173696A5085958014 @default.
• W1976173696 hasBestOaLocation W19761736961 @default.
• W1976173696 hasConcept C104317684 @default.
• W1976173696 hasConcept C153911025 @default.
• W1976173696 hasConcept C158617107 @default.
• W1976173696 hasConcept C167625842 @default.
• W1976173696 hasConcept C181199279 @default.
• W1976173696 hasConcept C185592680 @default.
• W1976173696 hasConcept C50476208 @default.
• W1976173696 hasConcept C515207424 @default.
• W1976173696 hasConcept C55493867 @default.
• W1976173696 hasConcept C71829478 @default.
• W1976173696 hasConcept C86803240 @default.
• W1976173696 hasConcept C96294017 @default.
• W1976173696 hasConceptScore W1976173696C104317684 @default.
• W1976173696 hasConceptScore W1976173696C153911025 @default.
• W1976173696 hasConceptScore W1976173696C158617107 @default.
• W1976173696 hasConceptScore W1976173696C167625842 @default.
• W1976173696 hasConceptScore W1976173696C181199279 @default.
• W1976173696 hasConceptScore W1976173696C185592680 @default.
• W1976173696 hasConceptScore W1976173696C50476208 @default.
• W1976173696 hasConceptScore W1976173696C515207424 @default.
• W1976173696 hasConceptScore W1976173696C55493867 @default.
• W1976173696 hasConceptScore W1976173696C71829478 @default.
• W1976173696 hasConceptScore W1976173696C86803240 @default.
• W1976173696 hasConceptScore W1976173696C96294017 @default.
• W1976173696 hasIssue "5" @default.
• W1976173696 hasLocation W19761736961 @default.
• W1976173696 hasLocation W19761736962 @default.
• W1976173696 hasOpenAccess W1976173696 @default.
• W1976173696 hasPrimaryLocation W19761736961 @default.
• W1976173696 hasRelatedWork W1761774275 @default.
• W1976173696 hasRelatedWork W1974824538 @default.
• W1976173696 hasRelatedWork W1976173696 @default.
• W1976173696 hasRelatedWork W1996865325 @default.
• W1976173696 hasRelatedWork W2008111244 @default.
• W1976173696 hasRelatedWork W2013190602 @default.
• W1976173696 hasRelatedWork W2028127774 @default.
• W1976173696 hasRelatedWork W2036398455 @default.
• W1976173696 hasRelatedWork W2041275422 @default.
• W1976173696 hasRelatedWork W2087062663 @default.
• W1976173696 hasVolume "18" @default.
• W1976173696 isParatext "false" @default.
• W1976173696 isRetracted "false" @default.
• W1976173696 magId "1976173696" @default.
• W1976173696 workType "article" @default.