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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