Results 211 to 220 of about 11,448 (264)
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Glucosidases and exo-glucanases
Canadian Journal of Biochemistry, 1968A comparison was made of exo-α-glucanases with α-glucosidases, and of exo-β1 → 3-glucanases with β-glucosidases to establish criteria for their characterization. Dimers, trimers, and tetramers of glucose are substrates for both exo-glucanases and glucosidases. Exo-glucanases act more rapidly on the longer oligomers, glucosidases on the shorter.
E T, Reese, A H, Maguire, F W, Parrish
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Immobilization of ?-D-Glucosidase and ?-D-Glucosidase-polyphenolic complexes
Biotechnology Letters, 1983β-D-Glucosidase, alone and after copolymerizing with a resorcinol polymer, was immobilized on a PM 10 ultrafiltration membrane, κ-carrageenan and DEAE (DE52) cellulose. The best support for both enzyme preparations, in terms of high Vmax values, was the ultrafiltration membrane.
Sarkar, J M, Burns, Richard G
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1994
Abstract Initial studies on partially purified a-glucosidase I from rat liver1·2 and oviduct microsomes3 .4 demonstrated that this enzyme removes a single glucose residue from Glc3Man9GlcNAc2. a-Glucosidase I was subsequently purified from calf5 and porcine6 liver, lactating bovine mammary tissue7, mung bean seedlings8, and 5 ...
R Trimble, K Moremcn,, A Herscovics
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Abstract Initial studies on partially purified a-glucosidase I from rat liver1·2 and oviduct microsomes3 .4 demonstrated that this enzyme removes a single glucose residue from Glc3Man9GlcNAc2. a-Glucosidase I was subsequently purified from calf5 and porcine6 liver, lactating bovine mammary tissue7, mung bean seedlings8, and 5 ...
R Trimble, K Moremcn,, A Herscovics
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Endocrinology and Metabolism Clinics of North America, 1997
Alpha-glucosidase inhibitors are antihyperglycemic agents that lower blood glucose by delaying the digestion and absorption of complex carbohydrates. They are competitive inhibitors of the enzymes in the brush border of enterocytes that cleave eligosaccharides to monosaccharides.
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Alpha-glucosidase inhibitors are antihyperglycemic agents that lower blood glucose by delaying the digestion and absorption of complex carbohydrates. They are competitive inhibitors of the enzymes in the brush border of enterocytes that cleave eligosaccharides to monosaccharides.
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A simple kinetic test to distinguish exo-glucosidase and β-glucosidase activities
Biochemical and Biophysical Research Communications, 1985Unusual kinetic behaviour was observed in assaying spectrophotometrically for exo-glucanase activity in a beta-glucosidase isolated from A. faecalis using p-nitrophenyl beta-cellobioside as substrate. At high substrate concentrations no phenol was released whereas at low concentrations a rapid release of phenol was detected and this increased in rate ...
A G, Day, S G, Withers
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The Determination of Amylo-1,6-Glucosidase
European Journal of Biochemistry, 1967Amylo-1,6-glucosidase has been measured by seven methods which have been compared. Some of them allow the separate determination of either the transglycosylation or of the hydrolytic step catalysed by the enzyme, whereas others measure the overall reaction. Their advantages and disadvantages are discussed.
H G, Hers, W, Verhue, F, Van hoof
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Reversible inhibitors of .beta.-glucosidase
Biochemistry, 1985A variety of reversible inhibitors of sweet almond beta-glucosidase were examined. These included simple sugars and sugar derivatives, amines and phenols. With respect to the sugar inhibitors and, indeed, the various glycoside substrates, the enzyme has what can be considered a "relaxed specificity".
M P, Dale +4 more
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A Spectrophotometric Assay for Glucosidase I
Analytical Biochemistry, 1994A spectrophotometric assay for glucosidase I using the synthetic trisaccharide alpha-D-Glc 1-->2 alpha-D-Glc 1-->3 alpha-D-Glc-O(CH2)8COOCH3 is reported. The terminal glucose is released from the substrate by the enzyme and quantitated using glucose oxidase, peroxidase, and o-dianisidine. The trisaccharide is specific for glucosidase I and provides all
I, Neverova +5 more
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The β-glucosidases of porcine kidney
Canadian Journal of Biochemistry, 1977Some of the properties of a partially purified particle bound and soluble β-glucosidase (EC 3.2.1.21) from pig kidney were compared. The soluble β-glucosidase (1) hydrolyzed 4-methylumbelliferyl-β-D-glucoside (4-MU-β-D-glucoside) 17α-estradiol 3β-glucoside, 17α-estradiol 17β-glucoside, and salicin, but not glucosylceramide, (2) possessed a broad pH ...
J N, Kanfer, R A, Mumford, S S, Raghavan
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Biochemistry. Biokhimiia, 2001
This review highlights the main properties of mammalian, plant, and microbial alpha-glucosidases. Special attention is given to the classification of these enzymes, possible catalytic mechanisms, their tertiary structure, and the structure of major inhibitors.
V V, Krasikov, D V, Karelov, L M, Firsov
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This review highlights the main properties of mammalian, plant, and microbial alpha-glucosidases. Special attention is given to the classification of these enzymes, possible catalytic mechanisms, their tertiary structure, and the structure of major inhibitors.
V V, Krasikov, D V, Karelov, L M, Firsov
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