The chick fibroblast cell surface after transformation by Rous sarcoma virus.
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Biomedical subjects
Publications and source records attributed to G G Wickus.
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A method for the partial purification of the pyruvate-uridine-diphospho-N-acetylglucosamine transferase from Staphylococcus epidermidis is presented. Some properties of the enzyme are discussed.
A method for the partial purification of the uridine diphospho-N-acetylglucosamine-enolpyruvate reductase from Staphylococcus epidermidis is presented. Some properties of the enzyme, including its dependence on monovalent cation and flavine adenine dinucleotide, are discussed.
Sindbis virus was iodinated by using the enzyme lactoperoxidase, an iodination technique which labels only surface proteins. By this technique, the two viral glycoproteins are labeled, and the internal viral protein is not. The two glycoproteins are iodinated to strikingly different extents. This difference in susceptibility to iodination apparently is due to the position or conformation of the glycoproteins in the envelope spikes of the virion and not to differing contents of tyrosine, the amino acid substrate of lactoperoxidase. Both viral glycoproteins are iodinated by lactoperoxidase on the surface of Sindbis-infected chicken cells. Here, as in the virion, the glycoproteins are iodinated unequally, with the smaller glycoprotein again being preferentially iodinated. Another virus-specific protein found in large amounts in infected cells, and from which the preferentially iodinated virion glycoprotein is produced by a proteolytic cleavage, is not iodinated by lactoperoxidase. Thus it appears that the viral glycoproteins are present on the cell surface and that the precursor protein is not.
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Evidence is presented for the appearance of muramic lactam during the late stages of sporulation at about the same time dipicolinic acid synthesis occurs.
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