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http://hdl.handle.net/10261/23880
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dc.contributor.author | Boscá, Lisardo | - |
dc.contributor.author | Morán, Federico | - |
dc.date.accessioned | 2010-05-04T09:22:44Z | - |
dc.date.available | 2010-05-04T09:22:44Z | - |
dc.date.issued | 1993 | - |
dc.identifier.citation | Biochemical Journal 290(3): 827-832 (1993) | en_US |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://hdl.handle.net/10261/23880 | - |
dc.description | 6 pages, 6 figures, 1 table. | en_US |
dc.description.abstract | The structural changes following the binding to protein kinase C (PKC) of activators that promote its translocation to lipid environments were studied by far-u.v. c.d. and intrinsic fluorescence measurements of the protein. In the absence of activators, PKC contained 40% alpha-helix, with an average size of 13 amino acids per alpha-helix segment, and 12% beta-structure as deduced from c.d. spectral analysis while fitting a set of model proteins of known structure. Ligands that promote translocation and activation of the enzyme, such as Ca2+ ions and phorbol esters, produced drastic changes in the c.d. spectra which may be interpreted as a reduction in the average number of consecutive amino acids in the alpha-helix. Most of the total alpha-helix structure was conserved and an increase in beta-structure was produced by active phorbol esters. These activators differentially affected the fluorescence of PKC: phorbol esters shifted the emission maximum to the red, whereas Ca2+ produced a marked decrease in the intensity of the fluorescence emission, suggesting in both cases that tryptophan residues were exposed to increased polar environments after binding of the ligands. | en_US |
dc.description.sponsorship | This work was supported by grant PM88025 and PB890108 from CICYT, Spain | en_US |
dc.format.extent | 1282924 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | Portland Press | en_US |
dc.rights | openAccess | en_US |
dc.title | Circular dichroism analysis of ligand-induced conformational changes in protein kinase C. Mechanism of translocation of the enzyme from the cytosol to the membranes and its implications | en_US |
dc.type | artículo | en_US |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://www.biochemj.org/bj/290/bj2900827.htm | en_US |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.fulltext | With Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.languageiso639-1 | en | - |
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2900827.pdf | 1,25 MB | Adobe PDF | Visualizar/Abrir |
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