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- W2093798522 abstract "Abstract The receptor for hemagglutinating enteroviruses on human erythrocytes was solubilized by butanol extraction in the presence of high concentration of CaCl2. The soluble material was further purified by precipitation of lipids with polyanions, gel filtration on Sephadex G-200, and isodensity centrifugation in CsCl. The soluble receptor which was purified 100 times from the membrane suspension had a buoyant density of 1.18, a S20o,w of 14 Svedberg units, and contained approximately 31% lipid, 60% protein, and 9% carbohydrate. The greater part of the lipid is probably a neutral glycolipid, but phospholipids and cholesterol were also present. A deoxypolynucleotide material containing the bases adenine, thymine, cytosine, and guanine in the ratios 1:1:0.5:0.9 is firmly attached to the receptor structure. Eight hemagglutinating units of ECHO 7, ECHO 19, or Coxsackie B3 virus are inhibited by 0.1–0.3 μg of the purified receptor. The effect against myxoviruses is 1000 times lower. The infectivity of hemagglutinating enteroviruses is irreversibly inactivated by the purified receptor, which does not affect the infectivity of nonhemagglutinating enteroviruses." @default.
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- W2093798522 date "1964-04-01" @default.
- W2093798522 modified "2023-09-27" @default.
- W2093798522 title "Purification and chemical analysis of the erythrocyte receptor for hemagglutinating enteroviruses" @default.
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- W2093798522 doi "https://doi.org/10.1016/0042-6822(64)90080-7" @default.
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