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http://hdl.handle.net/10261/23919
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dc.contributor.author | Mingorance, Jesús | - |
dc.contributor.author | Álvarez, Luis | - |
dc.contributor.author | Sánchez-Góngora, Estrella | - |
dc.contributor.author | Mato, José M. | - |
dc.contributor.author | Pajares, María A. | - |
dc.date.accessioned | 2010-05-05T08:35:59Z | - |
dc.date.available | 2010-05-05T08:35:59Z | - |
dc.date.issued | 1996-05-01 | - |
dc.identifier.citation | Biochemical Journal 315(3): 761-766 (1996) | en_US |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://hdl.handle.net/10261/23919 | - |
dc.description | 6 pages, 5 figures, 2 tables. | en_US |
dc.description.abstract | We have examined the functional importance of the cysteine residues of rat liver S-adenosylmethionine synthetase. For this purpose the ten cysteine residues of the molecule were changed to serines by site-directed mutagenesis. Ten recombinant enzyme mutants were obtained by using a bacterial expression system. The same level of expression was obtained for the wild type and mutants, but the ratio of S-adenosylmethionine synthetase between soluble and insoluble fractions differed for some of the mutant forms. The immunoreactivity against an anti-(rat liver S-adenosylmethionine synthetase) antibody was equivalent in all the cases. Effects on S-adenosylmethionine synthetase activities were also measured. Mutants C57S, C69S, C105S and C121S showed decreased relative specific activity of 68, 85, 63 and 29%, respectively, compared with wild-type, whereas C312S resulted in an increase of 1.6-fold. Separation of tetramer and dimer forms for wild type and mutants was carried out by using phenyl-Sepharose columns. The dimer/tetramer ratio was calculated based on the activity and on the protein level estimated by immunoblotting. No monomeric forms of the enzyme were detected in any case. Comparison of dimer/tetramer ratios indicates the importance of cysteine-69 (dimer/tetramer protein ratio of 88 versus 10.2 in the wild type) in maintaining the oligomeric state of rat liver S-adenosylmethionine synthetase. Moreover, all the mutations carried out of cysteine residues between cysteine-35 and cysteine-105 altered the ratio between oligomeric forms. | en_US |
dc.description.sponsorship | J.M. and E. S.-G. are fellows of the Ministerio de Educación y Ciencia and Comunidad de Madrid respectively. This work was supported by grants from the Fondo de Investigaciones Sanitarias (94/0231), Boehringer Ingelheim España and the Science Programme of the European Community (SCI*-CT92-0780). | en_US |
dc.format.extent | 445209 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | Portland Press | en_US |
dc.publisher | Biochemical Society | - |
dc.rights | closedAccess | en_US |
dc.title | Site-directed mutagenesis of rat liver S-adenosylmethionine synthetase | en_US |
dc.title.alternative | Identification of a cysteine residue critical for the oligomeric state | - |
dc.type | artículo | en_US |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://www.biochemj.org/bj/315/0761/bj3150761.htm | en_US |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
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