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- W2073193885 abstract "Abstract A simple, rapid procedure is described for eliminating protease contaminants from commercially available neuraminidase by affinity adsorption to celluloseimmobilized fetuin. Neuraminidase activity is enriched 10- to 25-fold depending on the enzyme source. Recovery of activity from batchwise adsorption is approximately 60%, while column chromatography recovery is better than 95%. Affinityadsorbed neuraminidase is virtually free of protease activity when evaluated using [ 3 H]hemoglobin as a substrate. The affinity adsorbent can be reused after elution of the enzyme, and defined proteases such as trypsin and pronase do not bind under experimental conditions. The analytical value of protease-free neuraminidase is discussed in relation to studies of the biological fates of desialated glycoproteins and tumor cells." @default.
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- W2073193885 date "1976-03-01" @default.
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- W2073193885 title "Preparation of protease-free neuraminidase by affinity adsorption on fetuin-derivatized cellulose" @default.
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- W2073193885 doi "https://doi.org/10.1016/0003-2697(76)90037-3" @default.
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