A folding study of Antarctic krill (Euphausia superba) alkaline phosphatase using denaturants

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dc.contributor.authorZ J Wang-
dc.contributor.authorJinhyuk Lee-
dc.contributor.authorY X Si-
dc.contributor.authorW Wang-
dc.contributor.authorJ M Yang-
dc.contributor.authorS J Yin-
dc.contributor.authorG Y Qian-
dc.contributor.authorY D Park-
dc.date.accessioned2017-04-19T09:55:27Z-
dc.date.available2017-04-19T09:55:27Z-
dc.date.issued2014-
dc.identifier.issn0141-8130-
dc.identifier.uri10.1016/j.ijbiomac.2014.07.001ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12122-
dc.description.abstractTo gain insight into the structural and folding mechanisms of Antarctic krill alkaline phosphatase (ALP), the enzyme was properly purified by (NH4)2SO4 fractionation and by both Sephadex G-75 and DEAE anion exchange chromatography. The purified enzyme (62.6kDa; 2.62unit/mg) was unstable at temperatures exceeding 30°C. Denaturants, such as sodium dodecyl sulfate (SDS), guanidine HCl, and urea, were applied to evaluate the folding mechanism, including kinetics and thermodynamics, of krill ALP. Sodium dodecyl sulfate elicited no significant effect on ALP activity even at excessively high concentrations (300mM), whereas guanidine HCl and urea effectively inactivated the enzyme at concentrations of 2 and 3.5M, respectively. Kinetic studies showed that the enzymatic inhibition by guanidine HCl and urea represented a first-order reaction that was a monophasic unfolding process. This process was found to be associated with conformational changes without significant transient free-energy changes. Additionally, the overall structural changes occurred proximally to the active site pocket. Our study provides new insight into ALP of the Antarctic krill, which lives in extreme environmental conditions.-
dc.publisherElsevier-
dc.titleA folding study of Antarctic krill (Euphausia superba) alkaline phosphatase using denaturants-
dc.title.alternativeA folding study of Antarctic krill (Euphausia superba) alkaline phosphatase using denaturants-
dc.typeArticle-
dc.citation.titleInternational Journal of Biological Macromolecules-
dc.citation.number0-
dc.citation.endPage274-
dc.citation.startPage266-
dc.citation.volume70-
dc.contributor.affiliatedAuthorJinhyuk Lee-
dc.contributor.alternativeNameWang-
dc.contributor.alternativeName이진혁-
dc.contributor.alternativeNameSi-
dc.contributor.alternativeNameWang-
dc.contributor.alternativeName양준모-
dc.contributor.alternativeNameYin-
dc.contributor.alternativeNameQian-
dc.contributor.alternativeName박용두-
dc.identifier.bibliographicCitationInternational Journal of Biological Macromolecules, vol. 70, pp. 266-274-
dc.identifier.doi10.1016/j.ijbiomac.2014.07.001-
dc.subject.keywordAlkaline phosphatase-
dc.subject.keywordAntarctic krill-
dc.subject.keywordFolding-
dc.subject.localAlkaline phosphatase-
dc.subject.localalkaline phosphatase-
dc.subject.localAntarctic krill-
dc.subject.localFolding-
dc.description.journalClassY-
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Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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