Comparative study of enzyme activity and stability of bovine and human plasmins in electrophoretic reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea

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dc.contributor.authorNack Shick Choi-
dc.contributor.authorJeung Ho Hahm-
dc.contributor.authorP J Maeng-
dc.contributor.authorSeung Ho Kim-
dc.date.accessioned2017-04-19T09:02:41Z-
dc.date.available2017-04-19T09:02:41Z-
dc.date.issued2005-
dc.identifier.issn1225-8687-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6910-
dc.description.abstractEffects of common electrophoretic reagents, reducing agents (β-mercaptoethanol [BME] and DTT), denaturants (SDS and urea), and non-ionic detergent (Triton X-100), on the activity and stability of bovine plasmin (b-pln) and human plasmin (h-pln) were compared. In the presence of 0.1% SDS (w/v), all reagents completely inhibited two plns, whereas SDS (1%) and urea (1 M) denatured plns recovered their activities after removal of SDS by treatment of 2.5% Triton X-100 (v/v). However, reducing agents (0.1 M of BME and DTT) treated plns did not restore their activities. Based on a fibrin zymogram gel, five (from b-pln) and four (from h-pln) active fragments were resolved. Two plns exhibited unusual stability in concentrated SDS and Triton X-100 (final 10%) and urea (final 6 M) solutions. Two bands, heavy chain-2 (HC-2) and cleaved heavy chain-2 (CHC-2), of b-pln were completely inhibited in 0.5% SDS or 3 M urea, whereas no significant difference was found in h-pln. Interestingly, 50 kDa (cleaved heavy chain-1, CHC-1) of b-pln and two fragments, 26 kDa (light chain, LC) and 29 kDa (microplasmin, MP), of h-pln were increased by SDS in a concentration dependent manner. We also found that the inhibition of SDS against both plns was reversible.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleComparative study of enzyme activity and stability of bovine and human plasmins in electrophoretic reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea-
dc.title.alternativeComparative study of enzyme activity and stability of bovine and human plasmins in electrophoretic reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number2-
dc.citation.endPage181-
dc.citation.startPage177-
dc.citation.volume38-
dc.contributor.affiliatedAuthorNack Shick Choi-
dc.contributor.affiliatedAuthorJeung Ho Hahm-
dc.contributor.affiliatedAuthorSeung Ho Kim-
dc.contributor.alternativeName최낙식-
dc.contributor.alternativeName함정호-
dc.contributor.alternativeName맹필재-
dc.contributor.alternativeName김승호-
dc.identifier.bibliographicCitationBMB Reports, vol. 38, no. 2, pp. 177-181-
dc.subject.keyworddenaturant-
dc.subject.keywordfibrin plate-
dc.subject.keywordfibrinolysis-
dc.subject.keywordplasmin-
dc.subject.keywordzymography-
dc.subject.localdenaturant-
dc.subject.localfibrin plate-
dc.subject.localfibrinolysis-
dc.subject.localFibrinolysis-
dc.subject.localplasmin-
dc.subject.localZymography-
dc.subject.localzymography-
dc.description.journalClassY-
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