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Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe
Author(s) -
Arbesú Ma José,
Valle Eulalia,
SuárezRendueles Paz
Publication year - 1993
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320090610
Subject(s) - schizosaccharomyces pombe , aminopeptidase , size exclusion chromatography , enzyme , biology , gel electrophoresis , biochemistry , polyacrylamide gel electrophoresis , sodium dodecyl sulfate , yeast , dimer , molecular mass , chromatography , schizosaccharomyces , amino acid , leucine , chemistry , saccharomyces cerevisiae , organic chemistry
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.