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Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe
dc.contributor.author | Arbesú, María José | |
dc.contributor.author | Valle Garay, Eulalia | |
dc.contributor.author | Suárez Rendueles, María Paz | |
dc.date.accessioned | 2014-11-28T11:06:06Z | |
dc.date.available | 2014-11-28T11:06:06Z | |
dc.date.issued | 1993 | |
dc.identifier.citation | Yeast, 9(6), p. 637–644 (1993); doi:10.1002/yea.320090610 | |
dc.identifier.issn | 0749-503X | |
dc.identifier.issn | 1097-0061 | |
dc.identifier.uri | http://hdl.handle.net/10651/28897 | |
dc.description.abstract | Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium dodecyl sulfate–polyacrylamide gel electrophoresis. The enzyme is thus a dimer with two identical subunits. Optimum pH for cleavage of synthetic aminoacyl-4-nitroanilides is 7·0. Mercury ions, EDTA and chloroquine were found to be potent inhibitors of aminopeptidase yspI activity. Substrate specificity studies indicate that the purified enzyme cleaves L-lysine-4-nitroanilide with high efficiency | en |
dc.format.extent | p. 637-644 | spa |
dc.language.iso | eng | spa |
dc.publisher | Wiley | |
dc.relation.ispartof | Yeast, 9(6) | spa |
dc.title | Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe | en |
dc.type | journal article | |
dc.identifier.doi | 10.1002/yea.320090610 | |
dc.relation.publisherversion | http://dx.doi.org/10.1002/yea.320090610 |
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