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- W2008608296 abstract "Abstract 1. 1. β-N-Acetylglucosaminidase was partially purified from the digestive gland of the three coastal New England bivalves Mercenaria mercenaria Spisula solidissuma and Mya arenaria and their properties compared. 2. 2. Heat inactivation studies on the β-N-acetylglucosaminidases preincubated at 45°C revealed that the preparation from S. solidissima was stable up to 60 min, while thatfrom M. arenaria and M. mercenaria lost 47 and 91% of their original activities under these conditions, respectively. 3. 3. Inhibition studies indicated that d -glucoronolactone is more inhibitory iswards the M. arenaria enzyme, while HgCI2 appears to be less inhibitory towards the S. solidissima enzyme. 4. 4. The Vmax value for β-N-acetylglucosaminidase from M. mercenaria was approximately 2.5 fold greater than that from S. solidissima and M. arenaria 5. 5. Other characteristics of the β-N-acetylglucosaminidases such as pH optimum Km, mol. wt, energy of activation, and effect of ionic strengtt on enzyme activity were found to be aimilar for all three species. 6. 6. The digestive gland of all three species of clams also contained the following activities: β- d - galactosidase, α- d -galactosidase, α- l -fucosidase, α-N-acetylgalactosaminidase and α- d -mannosidase. Trace amounts of β- d -xylosidase, α- d -xylosidase, α- d -glucosidase and β- d -glucuronidase were also detected." @default.
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- W2008608296 date "1981-01-01" @default.
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- W2008608296 title "A comparative study of β-N-acetylglucosamididase from Mercenaria mercenaria, Mya arenaria and Spisula solidissima" @default.
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- W2008608296 doi "https://doi.org/10.1016/0305-0491(81)90323-0" @default.
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