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- W2036426995 endingPage "1578" @default.
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- W2036426995 abstract "Mouse liver beta-glucuronidase is stabilized within microsomal vesicles by complexation with the accessory protein egasyn. The location of the beta-glucuronidase-egasyn complex and free egasyn within microsomal vesicles was investigated. Surprisingly, it was found that neither the complex nor free egasyn are intrinsic membrane components. Rather, both are either free within the vesicle lumen or only weakly bound to the inside of the vesicle membrane. This conclusion was derived from release studies using low concentrations of Triton X-100 or controlled sonication. Both the intact complex and free egasyn were released in parallel with lumenal proteins, not with intrinsic membrane components. Also, beta-glucuronidase was protected from digestion by proteinase K by the membrane of microsomal vesicles. The hydrophilic nature of both the complex and free egasyn was confirmed by phase separation experiments with the detergent Triton X-114. Egasyn is one of an unusual group of esterases that, despite being located within the lumen or only weakly bound to the lumenal surface of the endoplasmic reticulum, do not enter the secretory pathway." @default.
- W2036426995 created "2016-06-24" @default.
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- W2036426995 date "1987-10-01" @default.
- W2036426995 modified "2023-09-26" @default.
- W2036426995 title "Lumenal location of the microsomal beta-glucuronidase-egasyn complex." @default.
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- W2036426995 doi "https://doi.org/10.1083/jcb.105.4.1571" @default.
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