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http://hdl.handle.net/10261/18197
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Neptuno-Rodríguez, José | - |
dc.contributor.author | Espín de Gea, Juan Carlos | - |
dc.contributor.author | Amor, Francisco del | - |
dc.contributor.author | Tudela, José | - |
dc.contributor.author | Martínez, Vicente | - |
dc.contributor.author | Cerdá, Antonio | - |
dc.contributor.author | García-Cánovas, Francisco | - |
dc.date.accessioned | 2009-10-30T09:32:18Z | - |
dc.date.available | 2009-10-30T09:32:18Z | - |
dc.date.issued | 2000-04-18 | - |
dc.identifier.citation | Journal of Agricultural and Food Chemistry 48(5): 1537-1541 (2000) | en_US |
dc.identifier.issn | 0021-8561 | - |
dc.identifier.uri | http://hdl.handle.net/10261/18197 | - |
dc.description | 5 pages, 6 figures, 1 table. | en_US |
dc.description.abstract | The partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography in the purification scheme. The sample obtained was used to characterize MPX. This peroxidase did not show activity on ascorbic acid but oxidized guaiacol at a high rate, showing an optimum pH of 5.5 when acting on this last reducing substrate. Melon fruits grown under highly saline conditions showed slightly increased levels of this anionic isoenzyme. Kinetic studies using 2,2‘-azinobis(3-ethylbenzothiazolinesulfonic acid) (ABTS) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameters of melon peroxidase on both hydrogen peroxide and reducing substrate. | en_US |
dc.description.sponsorship | This work was supported in part by a grant from the Comisión Interministerial de Ciencia y Tecnologia (CICYT), Spain, projects PB98- 0403-C02-01 and AGF95-0135. | en_US |
dc.format.extent | 259768 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | closedAccess | en_US |
dc.subject | Melon | en_US |
dc.subject | Peroxidase | en_US |
dc.subject | Salinity | en_US |
dc.subject | Peroxidase isoenzyme | en_US |
dc.subject | Enzyme kinetics | en_US |
dc.title | Purification and kinetic characterization of an anionic peroxidase from melon (Cucumis melo L.) cultivated under different salinity conditions | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1021/jf9905774 | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://dx.doi.org/10.1021/jf9905774 | en_US |
dc.identifier.e-issn | 1520-5118 | - |
dc.contributor.funder | Comisión Interministerial de Ciencia y Tecnología, CICYT (España) | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100007273 | es_ES |
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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