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- W1601355593 abstract "Abstract The solubilization of β-N- acetylglucosaminidase (β-2-acetamido-2-deoxy- d -glucoside acetamidodeoxyglucohydrolase, EC 3.2.1.30) has been investigated in subcellular preparations from rat liver and compared with that for other lysosomal hydrolases. The degree of retention of the enzyme activity by sedimentable material in lysosome-rich fractions largely varies depending on the disruptive procedure adopted. Solubilized enzyme added to “intact” homogenates is mostly adsorbed by sedimentable structures. After in vivo changes of lysosomes by Amanita phalloides poisoning, the activity recovered in the soluble fraction of the homogenate is almost negligible. In contrast, other lysosomal hydrolases display a pronounced shift from the particulate to the soluble phase. It is suggested that marked adsorption phenomena are likely to affect the distribution pattern of this enzyme activity in the situations examined." @default.
- W1601355593 created "2016-06-24" @default.
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- W1601355593 date "1971-05-01" @default.
- W1601355593 modified "2023-09-26" @default.
- W1601355593 title "On the structure-linked sedimentability of rat liver" @default.
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- W1601355593 doi "https://doi.org/10.1016/0005-2744(71)90214-2" @default.
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