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• W1586261795 abstract "The in vivo incorporation of exogenous radioactive acetate into two proteins of Sindbis virus, the capsid protein and PE2, is described. Under appropriate labeling conditions, 40-50% of the label in the capsid protein is found in an N-acetyl group which constitutes the NH_2-terminal modification of this blocked protein. The incorporated radiolabeled acetate was useful in the purification and analysis of peptides derived from the NH_2-terminus of the capsid protein, and from these peptides the NH_2-terminal sequence of the protein was determined to be N-acetyl-Met-Asx-, with the asx group most likely asparagine. The analysis of a peptide derived from the NH_2-terminus of PE2 and containing 45% of the acetate-derived label in this protein leads us to conclude that at least a significant fraction of PE2 is also blocked by N-acetylation." @default.
• W1586261795 created "2016-06-24" @default.
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• W1586261795 date "1981-08-01" @default.
• W1586261795 modified "2023-09-29" @default.
• W1586261795 title "In vivo NH2-terminal acetylation of Sindbis virus proteins." @default.
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• W1586261795 doi "https://doi.org/10.1016/s0021-9258(18)43379-0" @default.
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