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Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity

dc.contributor.authorArbesú, María José
dc.contributor.authorGascón Muñoz, Santiago 
dc.contributor.authorSuárez Rendueles, María Paz 
dc.date.accessioned2014-12-01T11:05:46Z
dc.date.available2014-12-01T11:05:46Z
dc.date.issued1991
dc.identifier.citationYeast, 7(5), p. 525–531 (1991); doi:10.1002/yea.320070512
dc.identifier.issn0749-503X
dc.identifier.issn1097-0061
dc.identifier.urihttp://hdl.handle.net/10651/28924
dc.description.abstractA mutant strain of the fission yeast Schizosaccharomyces pombe defective in aminopeptidase I was isolated by screening for lack of activity against the chromogenic substrate lysine-β-naphthlamide in isolated colonies. Tetrad dissection of sporulated diploids heterozygous for the wild-type and mutant allele resulted in a 2:2 segregation of mutant and wild-type phenotype indicating a single chromosomal gene mutation. Gene dosage experiments indicated that the mutation might reside in the structural gene of aminopeptidase I. No vital consequences of aminopeptidase I deficiency on cell life and sporulation could be detected. However, the enzyme seems to be involved in protein degradation under conditions of nutrient deprivationspa
dc.format.extentp. 525-531spa
dc.language.isoengspa
dc.publisherWiley
dc.relation.ispartofYeast, 7 (5)spa
dc.titleIsolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activityspa
dc.typejournal article
dc.identifier.doi10.1002/yea.320070512
dc.relation.publisherversionhttp://dx.doi.org/10.1002/yea.320070512


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