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  • Title: Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe.
    Author: Arbesú MJ, Valle E, Suárez-Rendueles P.
    Journal: Yeast; 1993 Jun; 9(6):637-44. PubMed ID: 8346680.
    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.
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