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• W2028814643 abstract "A neutral β-galactosidase has been purified by concanavalin A-Sepharose affinity chromatography, DEAE-cellulose chromatography, Sephadex G-200 gel filtration and hydroxylapatite chromatography. The enzyme was purified 126-fold with a yield of about 21%. This form has a neutral optimal pH (7.5) and it is located in the cytosolic fraction. It shows a wide pH stability from pH 4.5 to 8.0, but it is very unstable at low pH values. Its isoelectric point is 4.9 and this value does not change on neuraminidase treatment. The estimated molecular weight was 47 000. The neutral form shows β-d-galactosidase, β-d-fucosidase and β-d-glucosidase activities, all of them associated in a single peak in all the purification steps. p-Nitrophenyl β-d-galactosides, p-nitrophenyl β-d-fucosides and p-nitrophenyl β-d-glucosides competed fully for a common active site in mixed-substrate experiments. Using γ-d-galactonolactone as competitive inhibitor the Ki values were always coincident for the three activities. The effect of NaCl, methyl mannoside and some sugars (fucose, galactose and glucose) was studied. Une isoenzyme de β-d-galactosidase de rein de lapin a été localisée dans le cytosol et elle a un caractère neutre, avec un pH optimum de 7,5 et un point isoélectrique de 4,9. La valeur du point isoélectrique ne se modifie pas après traitement par la neuraminidase. L'enzyme est stable pour des valeurs de pH comprises entre 4,5 et 8,0. Par filtration sur gel de Sephadex G-200 elle ne donne qu'un seul pic d'activité dont la masse moléculaire estimée est de 47 000. Cette forme de l'enzyme a été purifiée 126 fois après 4 étapes de purification avec un rendement du 21%. Des activités β-d-fucosidasique et β-d-glucosidasique sont toujours associées à l'activité β-d-galactosidasique. Les substrats pNPh-β-d-galactoside, pNPh-β-d-glucoside et pNPh-β-d-fucoside sont en compétition pour le site actif de l'enzyme d'après les expériences où l'on utilise un mélange des trois substrats. Le fucose et la γ-d-galactonolactone sont des inhibiteurs compétitifs dont les valeurs de Ki sont identiques pour chacune des trois activités. L'effet du ClNa du méthyl-mannoside et de certains sucres (fucose, galactose et glucose) a été étudié." @default.
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• W2028814643 date "1986-03-01" @default.
• W2028814643 modified "2023-10-15" @default.
• W2028814643 title "Properties and kinetics of a neutral β-galactosidase from rabbit kidney" @default.
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• W2028814643 doi "https://doi.org/10.1016/s0300-9084(86)80022-0" @default.
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