Partial purification and characterization of alpha-glucosidase from Pseudomonas fluorescens W |
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Authors: | Arthur A. Guffanti W. A. Corpe |
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Affiliation: | (1) Department of Biological Sciences, Columbia University, 1305 Altschul Hall, 10027 New York, New York, USA;(2) Department of Biochemistry, Mt. Sinai School of Medicine, Fifth Ave. and 100th St., 10029 New York, N.Y., USA |
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Abstract: | The -glucosidase (-d-glucoside glucohydrolase, EC 3.2.1.20) of Pseudomonas fluorescens W was partially purified by (NH4)2SO4 fractionation, Sephadex G-200 and DEAE-cellulose column chromatography. The enzyme showed great specificity for maltose hydrolysis, with very little action against polymeric forms. Sucrose, isomaltose, -methylglucoside, and maltobionic acid were not hydrolyzed. Turanose was a strong competitive inhibitor, and glucose a weaker one. Tris (2-amino-2-hydroxymethylpropan-1:3-diol) inhibited enzyme activity significantly only at alkaline pH. Mercuric, cupric, and silver cations strongly inhibited, and EDTA (ethylenediaminetetraacetate) weakly inhibited the enzyme. The isolated enzyme was rather unstable even at 4° C, and was destroyed by freezing and lyophilization. Inositol and albumin had a slightly protective effect. Sulfhydryl-binding reagents strongly inhibited the enzyme.Abbreviations PNPG paranitrophenyl--d-glucoside - PCMB parachloromercuribenzoate - DEAE diethylaminoethyl cellulose - NEM N-ethylmaleimide - EDTA ethylenediaminetetraacetate |
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Keywords: | Pseudomonas fluorescens W Maltose hydrolysis /content/g66q76511p848276/xxlarge945.gif" alt=" agr" align=" BASELINE" BORDER=" 0" >-Glucosidase-partial purification |
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