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- W2083241504 abstract "Abstract Here we have characterized the oligosaccharide chains of the viral membrane proteins from chicken embryo fibroblasts infected with ts 1 mutant of Semliki Forest virus. When the infected cells were labeled with [ 3 H]mannose and maintained at 39°, the radioactive oligosaccharides were exclusively of the high mannose type as evidenced by their sensitivity to endoglycosidase H and their high affinity to immobilized concanavalin A. When the infected cells were labeled at 39° followed by chase at 28° in the presence of cycloheximide, about 35% of the high mannose type oligosaccharides were converted to complex oligosaccharides as evidenced by their elution behavior from concanavalin A-Sepharose, resistance to endoglycosidase H, and sensitivity to mild acid hydrolysis. The rest of the oligosaccharides remained as high mannose type chains. The results suggest that at the restrictive temperature the viral membrane glycoproteins in ts -1 infected cells are arrested in the rough endoplasmic reticulum, but start to be transported to the Golgi complex, once the cultures are shifted to the permissive temperature." @default.
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- W2083241504 date "1981-02-01" @default.
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- W2083241504 title "Reversible defect in the glycosylation of the membrane proteins of Semliki forest virus ts-1 mutant" @default.
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- W2083241504 doi "https://doi.org/10.1016/0042-6822(81)90481-5" @default.
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