dc.creator | Losada Villasante, Manuel | |
dc.creator | Serrano Delgado, Aurelio | |
dc.creator | Rivas Florido, Joaquín | |
dc.date.accessioned | 2015-06-24T11:06:50Z | |
dc.date.available | 2015-06-24T11:06:50Z | |
dc.date.issued | 1984 | |
dc.identifier.citation | Losada Villasante, M., Serrano Delgado, A. y Rivas Florido, J. (1984). Purification and properties of glutathione reductase from the cyanobacterium Anabaena sp. strain 7119. Journal of Bacteriology, 158 (1), 317-324. | |
dc.identifier.issn | 0021-9193 | es |
dc.identifier.uri | http://hdl.handle.net/11441/26063 | |
dc.description.abstract | An NADPH-glutathione reductase (EC 1.6.4.2) has been purified 6,000-fold to electrophoretic homogeneity
from the filamentous cyanobacterium Anabaena sp. strain 7119. The purified enzyme exhibits a specific
activity of 249 U/mg and is characterized by being a dimeric flavin adenine dinucleotide-containing protein
with a ratio of absorbance at 280 nm to absorbance at 462 nm of 5.8, a native molecular weight of 104,000, a
Stokes radius of 4.13 nm, and a pI of 4.02. The enzyme activity is inhibited by sulfhydryl reagents and
heavy-metal ions, especially in the presence of NADPH, with oxidized glutathione behaving as a protective
agent. As is the case with the same enzyme from other sources, the kinetic data are consistent with a
branched mechanism. Nevertheless, the cyanobacterial enzyme presents three distinctive features with
respect to that isolated from non-photosynthetic organisms: (i) absolute specificity for NADPH, (ii) an
alkaline optimum pH value of ca. 9.0, and (iii) strong acidic character of the protein, as estimated by column
chromatofocusing. The kinetic parameters are very similar to those found for the chloroplast enzyme, but
the molecular weight is lower, being comparable to that of non-photosynthetic microorganisms. A
protective function, analogous to that assigned to the chloroplast enzyme, is suggested. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Society for Microbiology | es |
dc.relation.ispartof | Journal of Bacteriology, 158 (1), 317-324. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Purification and properties of glutathione reductase from the cyanobacterium Anabaena sp. strain 7119 | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.publisherversion | http://jb.asm.org/content/158/1/317.full.pdf+html | es |
dc.journaltitle | Journal of Bacteriology | es |
dc.publication.volumen | 158 | es |
dc.publication.issue | 1 | es |
dc.publication.initialPage | 317 | es |
dc.publication.endPage | 324 | es |
dc.identifier.idus | https://idus.us.es/xmlui/handle/11441/26063 | |