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Glutathione S-transferase activities of S-Type and L-type thioltransferases from Arabidopsis thaliana

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dc.contributor.authorCho, YW-
dc.contributor.authorPark, EH-
dc.contributor.authorLim, CJ-
dc.date.available2021-02-22T16:47:21Z-
dc.date.created2020-09-01-
dc.date.issued2000-03-31-
dc.identifier.issn1225-8687-
dc.identifier.urihttps://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16775-
dc.description.abstractThe glutathione S-transferase (GST) activities of S-type and L-type thioltransferases (TTases), which are purified from the seeds and leaves of Arabidopsis thaliana, respectively, were identified and compared. The S-type and L-type TTases showed K-m, values of 9.72 mM and 3.18 mM on 1-chloro-2,4-dinitrobenzene (CDNB), respectively, indicating the L-type TTase has higher affinity for CDNB. The GST activity of the L-type TTase was rapidly inactivated after being heated at 70 degrees C or higher. The GST activity of the S-type TTase remains active in a range of 30-90 degrees C. Hg2+ inhibited the GST activity of the S-type TTase, whereas Ca2+ and Cd2+ inhibited the GST activity of the L-type TTase. Our results suggest that the GST activities of two TTases of Arabidopsis thaliana may have different catalytic mechanisms. The importance of the co-existence of TTase and GST activities in one protein remains to be elucidated.-
dc.language영어-
dc.language.isoen-
dc.publisherSPRINGER-VERLAG SINGAPORE PTE LTD-
dc.subjectESCHERICHIA-COLI-
dc.subjectPURIFICATION-
dc.subjectGLUTAREDOXIN-
dc.subjectIDENTIFICATION-
dc.subjectREDUCTASE-
dc.subjectPLANT-
dc.titleGlutathione S-transferase activities of S-Type and L-type thioltransferases from Arabidopsis thaliana-
dc.typeArticle-
dc.contributor.affiliatedAuthorPark, EH-
dc.identifier.scopusid2-s2.0-0000334134-
dc.identifier.wosid000086149800013-
dc.identifier.bibliographicCitationJOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.33, no.2, pp.179 - 183-
dc.relation.isPartOfJOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY-
dc.citation.titleJOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY-
dc.citation.volume33-
dc.citation.number2-
dc.citation.startPage179-
dc.citation.endPage183-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusPURIFICATION-
dc.subject.keywordPlusGLUTAREDOXIN-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusREDUCTASE-
dc.subject.keywordPlusPLANT-
dc.subject.keywordAuthorArabidopsis thaliana-
dc.subject.keywordAuthorglutaredoxin-
dc.subject.keywordAuthorglutathione S-transferase-
dc.subject.keywordAuthorthioltransferase-
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