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- W2010814343 abstract "The paramyxovirus glycoprotein which is required for virus-induced cell fusion, hemolysis, and the initiation of infection (F protein) has been found with three different viruses to consist of two disulfide-linked glycopolypeptide chains (F1 and F2) which are derived from the precursor glycopolypeptide (F0) by proteolytic cleavage. The larger glycopolypeptide chain (F1) previously identified in SV5, Sendai, and Newcastle disease virions has an estimated molecular weight of 48,000–54,000. The smaller polypeptide chain (F2) has been found to have a molecular weight of ∼10,000–16,000, depending on the virus. The identification of the F2 polypeptide was accomplished by isolating the disulfide-linked complex (F1,2) under nonreducing conditions, followed by reduction of the disulfide bonds and separation of the two polypeptide chains. Although both polypeptides are glycosylated, the F2 polypeptide contains more carbohydrate per unit protein than F1. No free N-terminus could be detected on the F0 or F2 polypeptides of Sendai virus, whereas N-terminal phenylalanine was found on F1. This suggests that the order of the F0 polypeptide is X-NH-F2—Phe-F1—COOH. The finding that with three different paramyxoviruses the biologically active virions possess F1 and F2 polypeptides suggests that this is a general feature of paramyxoviruses, and that the activation of infectivity, cell fusion, and hemolysis is due to a conformational change in the F protein resulting from proteolytic cleavage to form an active complex of two disulfide-linked polypeptide chains." @default.
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- W2010814343 date "1977-07-01" @default.
- W2010814343 modified "2023-09-23" @default.
- W2010814343 title "Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses" @default.
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- W2010814343 doi "https://doi.org/10.1016/0042-6822(77)90380-4" @default.
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