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• W2013438400 abstract "Abstract An endoglycosidase H (Endo H) assay based on the use of a glycoprotein enzyme as substrate, in conjunction with immobilised concanavalin A (Con A), was devised and investigated. In this system, ribonuclease B (RNAase B) functions as both glycosidase substrate and reporter enzyme. Separation of glycosylated from deglycosylated RNAase B is effected by mixing with colloidal Con A-agarose, followed by centrifugation. The activity of carbohydrate-denuded RNAase B in the supernate is used to calculate endoglycosidase activity. Results obtained with this assay correlated closely with analysis of digest products by denaturing electrophoresis and lectin reactivity on western blots. Effective removal of non-hydrolysed RNAase B from assay digests was dependent on both lectin-agarose bead concentration and time of exposure. The assay was linear over the range 10–100 fmol of Endo H protein; a Km value of 0.48 mmol/l and turnover number of 7200 mol RNAase B/mol enzyme/min was determined for this endoglycosidas..." @default.
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• W2013438400 date "1997-04-01" @default.
• W2013438400 modified "2023-09-26" @default.
• W2013438400 title "Spectrophotometric Assay of Endo-β-N-acetylglucosaminidase H Activity" @default.
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• W2013438400 doi "https://doi.org/10.1080/00032719708004043" @default.
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