Purification and characterization of nitric oxide synthase from Staphylococcus aureus
DC Field | Value | Language |
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dc.contributor.author | Hong, Il-Sun | - |
dc.contributor.author | Kim, Yong Kee | - |
dc.contributor.author | Choi, Wahn Soo | - |
dc.contributor.author | Seo, Dong Wan | - |
dc.contributor.author | Yoon, Jong Woo | - |
dc.contributor.author | Han, Jeung-Whan | - |
dc.contributor.author | Lee, Hoi Yong | - |
dc.contributor.author | Lee, Hyang Woo | - |
dc.date.accessioned | 2022-04-19T12:04:44Z | - |
dc.date.available | 2022-04-19T12:04:44Z | - |
dc.date.issued | 2003-05 | - |
dc.identifier.issn | 0378-1097 | - |
dc.identifier.issn | 1574-6968 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/149164 | - |
dc.description.abstract | We previously reported the presence of nitric oxide synthase (NOS) in Staphylococcus aureus ATCC6538P whose activity was induced by methanol. In the present study, the methanol-induced NOS was purified 900-fold from S. aureus by means of Mono Q ion exchange column, 2′,5′-ADP-agarose affinity column, and Superdex 200HR gel permeation column chromatography. The purified bacterial NOS showed two protein bands with 67 and 64 kDa molecular mass on SDS-PAGE. However, the molecular mass of the NOS was 135 kDa on Superdex 200HR gel permeation column chromatography, indicating that the native enzyme exists as a heterodimer. This bacterial NOS had Km value of 13.4×10-6 M for L-arginine and Vmax of 35.3 nmol min-1 mg-1 protein. In addition, reduced nicotinamide adenine dinucleotide phosphate, flavin adenine dinucleotide, flavin mononucleotide, tetrahydrobiopterin, calmodulin and Ca2+ were required as cofactors in the conversion of L-arginine to L-citrulline, and NOS inhibitors selectively inhibited the activity of the purified NOS. © 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. | - |
dc.format.extent | 6 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Elsevier Science | - |
dc.title | Purification and characterization of nitric oxide synthase from Staphylococcus aureus | - |
dc.type | Article | - |
dc.publisher.location | 영국 | - |
dc.identifier.doi | 10.1016/S0378-1097(03)00254-4 | - |
dc.identifier.scopusid | 2-s2.0-0038397576 | - |
dc.identifier.wosid | 000183239100004 | - |
dc.identifier.bibliographicCitation | FEMS Microbiology Letters, v.222, no.2, pp 177 - 182 | - |
dc.citation.title | FEMS Microbiology Letters | - |
dc.citation.volume | 222 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 177 | - |
dc.citation.endPage | 182 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Nitric oxide synthase | - |
dc.subject.keywordAuthor | Purification | - |
dc.subject.keywordAuthor | Staphylococcus aureus | - |
dc.identifier.url | https://academic.oup.com/femsle/article/222/2/177/507059 | - |
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