DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김임숙 | ko |
dc.contributor.author | 곽주현 | ko |
dc.date.accessioned | 2010-09-09 | - |
dc.date.available | 2010-09-09 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1999-02 | - |
dc.identifier.citation | 전기화학회지, v.2, no.1, pp.27 - 30 | - |
dc.identifier.issn | 1229-1935 | - |
dc.identifier.uri | http://hdl.handle.net/10203/19339 | - |
dc.description.abstract | Self-Assembled monolayers of carboxyl-terminated alkanethiols, which is negatively charged in pH 7.0, were usually used to facilitate the electron transfer between the positively charged protein and the electrode. In case of L-cysteine, as it has both positive and negative group, it can be a candidate for a new modifier to facilitate positively charged protein or negatively charged protein. Our investigation of L-cysteine shows that the electron transfer occurs successfully to both cytochrome c (cyt. c) and pyrroloquinoline quinone (PQQ). By using 1-ethyl-3-(3-dime-thlyaminopropyl) carbodiimide (EDC), we made a covalent bond between cyt. c and monolayer. Then PQQ was electrostatically adsorbed to the same monolayer. Cyclic voltammograms show that both molecules do not interfere each other and electron transfer is appreciable. | - |
dc.language | Korean | - |
dc.publisher | 한국전기화학회 | - |
dc.title | Investigation of the electrode reaction of cytochrome c and pyrroliquinoline quinone at self-assembled monolayers of amino acid | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.citation.volume | 2 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 27 | - |
dc.citation.endingpage | 30 | - |
dc.citation.publicationname | 전기화학회지 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | 곽주현 | - |
dc.contributor.nonIdAuthor | 김임숙 | - |
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