PROTEOLYSIS OF GLUCAGON BOUND TO DIMYRISTOYLPHOSPHATIDYLCHOLINE VESICLE

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dc.contributor.authorYi, Gwan-Suko
dc.contributor.authorKim, Hyoung Manko
dc.date.accessioned2010-03-10T02:23:37Z-
dc.date.available2010-03-10T02:23:37Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued1990-12-
dc.identifier.citationBULLETIN OF THE KOREAN CHEMICAL SOCIETY, v.11, no.6, pp.534 - 538-
dc.identifier.issn0253-2964-
dc.identifier.urihttp://hdl.handle.net/10203/17067-
dc.description.abstractGlucagon was found to interact with DMPC vesicles electrostatically and hydrophobically. It appears that glucagon bound irreversibly to the vesicles through hydrophobic interaction was partially protected from the proteolysis by trypsin. Out of three possible sites, only the peptide bond preceded by Arg-18 was cleaved by a prolonged trypsintreatment. alpha-chymotrysin did not affect the vesicle-bound glucagon. Based on these observations, possible structure of irreversibly bound glucagon on the vesicle surface is discussed.-
dc.languageEnglish-
dc.language.isoen_USen
dc.publisherKOREAN CHEMICAL SOC-
dc.subjectPHOSPHOLIPID-VESICLES-
dc.subjectALPHA-LACTALBUMIN-
dc.subjectCONFORMATION-
dc.subjectHORMONES-
dc.subjectFUSION-
dc.titlePROTEOLYSIS OF GLUCAGON BOUND TO DIMYRISTOYLPHOSPHATIDYLCHOLINE VESICLE-
dc.typeArticle-
dc.identifier.wosidA1990EV68600021-
dc.type.rimsART-
dc.citation.volume11-
dc.citation.issue6-
dc.citation.beginningpage534-
dc.citation.endingpage538-
dc.citation.publicationnameBULLETIN OF THE KOREAN CHEMICAL SOCIETY-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorYi, Gwan-Su-
dc.type.journalArticleArticle-
dc.subject.keywordPlusPHOSPHOLIPID-VESICLES-
dc.subject.keywordPlusALPHA-LACTALBUMIN-
dc.subject.keywordPlusCONFORMATION-
dc.subject.keywordPlusHORMONES-
dc.subject.keywordPlusFUSION-
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