Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

Non-ionic detergents Nonidet P-40 and Triton X-100 increase enzymatic activity of plasmin

Full metadata record
DC Field Value Language
dc.contributor.authorTrinh, Trang H. T.-
dc.contributor.authorKim, Jeeyoung-
dc.contributor.authorLee, Chul-Hoon-
dc.contributor.authorRyou, Chongsuk-
dc.date.accessioned2021-06-22T10:03:29Z-
dc.date.available2021-06-22T10:03:29Z-
dc.date.created2021-01-21-
dc.date.issued2019-04-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://scholarworks.bwise.kr/erica/handle/2021.sw.erica/3007-
dc.description.abstractPlasmin is a potent serin protease involved in a variety of biological functions, such as fibrinolysis and tissue remodeling. On performing an in vitro control assay to measure the activity of endogenous plasmin in cell lysates, a stimulatory effect of non-ionic detergent NP-40 on plasmin activity was discovered. Another non-ionic detergent, TX-100, also enhanced plasmin activity, while ionic detergents sodium deoxycholate and sodiem dodecyl sulfate abolished plasmin enzyme activity. Kinetic analysis of plasmin activity in the presence of NP-40 and TX-100 demonstrated an increase in V-max; however, there was no change in K-m values, suggesting that these detergents stimulate plasmin activity in a non-competitive manner. Fibrin plate assay indicates that NP-40 and TX-100 functionally stimulate plasmin activity by showing a dose-dependent increase in fibrinolysis. (C) 2019 Elsevier Inc. All rights reserved.-
dc.language영어-
dc.language.isoen-
dc.publisherAcademic Press-
dc.titleNon-ionic detergents Nonidet P-40 and Triton X-100 increase enzymatic activity of plasmin-
dc.typeArticle-
dc.contributor.affiliatedAuthorLee, Chul-Hoon-
dc.contributor.affiliatedAuthorRyou, Chongsuk-
dc.identifier.doi10.1016/j.bbrc.2019.03.052-
dc.identifier.scopusid2-s2.0-85062893727-
dc.identifier.wosid000468254400028-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, v.512, no.2, pp.314 - 318-
dc.relation.isPartOfBiochemical and Biophysical Research Communications-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.volume512-
dc.citation.number2-
dc.citation.startPage314-
dc.citation.endPage318-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.subject.keywordPlusFIBRINOLYSIS-
dc.subject.keywordPlusENHANCEMENT-
dc.subject.keywordPlusDISORDER-
dc.subject.keywordPlusSALTS-
dc.subject.keywordAuthorNon-ionic-
dc.subject.keywordAuthorDetergent-
dc.subject.keywordAuthorEnzyme-
dc.subject.keywordAuthorPlasmin-
dc.subject.keywordAuthorNon-competitive-
dc.subject.keywordAuthorStimulator-
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0006291X19304292?via%3Dihub-
Files in This Item
Go to Link
Appears in
Collections
COLLEGE OF PHARMACY > DEPARTMENT OF PHARMACY > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Ryou, Chong suk photo

Ryou, Chong suk
COLLEGE OF PHARMACY (DEPARTMENT OF PHARMACY)
Read more

Altmetrics

Total Views & Downloads

BROWSE