L Kaariainen

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Temperature-sensitive mutants of semliki forest virus (SFV) and sindbis virus (SIN) were used to study the intracellular transport of virus membrane glycoproteins in infected chicken embryo fibroblasts. When antisera against purified glycoproteins and (125)I- labeled protein A from staphylococcus aureus were used only small amounts of virus glycoproteins(More)
The human leukemia cell line K562 is erythroid and expresses the major red cell sialoglycoprotein, glycophorin A. With this cell line we have studied the biosynthesis of glycophorin A after pulse-chase labeling with [35S] methionine. Using lectin-Sepharose affinity chromatography and immune precipitation with specific anti-glycophorin A antiserum followed(More)
The phospholipids of Semliki Forest virus grown in mosquito cells (Aedes albopictus) were analyzed radiochemically. The ratio of 32P-labeled phospholipids to total 32P-label in the virus grown in mosquito cells equilibrated with radiophosphorus was 0.558 +/- 0.021. This value was similar to the lipid phosphorus: total phosphorus ratio (0.539 +/- 0.025) of(More)
When cells infected with the Semliki Forest virus (SFV) mutant ts-4 were shifted to the nonpermissive temperature, synthesis of 26S RNA ceased, whereas synthesis of 42S RNA continued normally. These two single-stranded SFV RNAs are synthesized in two types of replicative intermediate (RI), 26S RNA in RI(b) and 42S RNA in RI(a). Cessation of 26S RNA(More)
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