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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1971-5-17
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pubmed:abstractText |
The amino acid sequence of the membrane glycoprotein of Sindbis virus is specified by the viral genome, but it has not been determined whether the carbohydrate portion of this molecule is specified by the cell or by the virus. We have examined two of the enzyme activities which catalyze transfer of monosaccharides to glycoprotein (sialyl and fucosyl transferases). Comparison of particulate enzyme preparations from infected and uninfected cells showed no difference in either the specific activity or acceptor specificity of these enzymes. This is impressive in view of the fact that the Sindbis membrane glycoprotein is the only glycoprotein synthesized in the infected cell. It was also determined that sialyl transferase from uninfected cells is capable of transferring ((3)H) sialic acid to acceptor prepared from Sindbis membrane glycoprotein. These results imply that at least some of the carbohydrate of the virus glycoprotein can arise by host modification.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-13669336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-13672998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-14326976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-4301007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-4314902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-4320586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-4322870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-4908735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-5409648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-5418165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-5418166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-5777557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5102426-5911885
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
309-13
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:5102426-Acrylates,
pubmed-meshheading:5102426-Animals,
pubmed-meshheading:5102426-Arboviruses,
pubmed-meshheading:5102426-Centrifugation, Zonal,
pubmed-meshheading:5102426-Chick Embryo,
pubmed-meshheading:5102426-Culture Techniques,
pubmed-meshheading:5102426-Electron Transport,
pubmed-meshheading:5102426-Electrophoresis,
pubmed-meshheading:5102426-Fibroblasts,
pubmed-meshheading:5102426-Fucose,
pubmed-meshheading:5102426-Gels,
pubmed-meshheading:5102426-Genetics, Microbial,
pubmed-meshheading:5102426-Glucosyltransferases,
pubmed-meshheading:5102426-Glycols,
pubmed-meshheading:5102426-Glycoproteins,
pubmed-meshheading:5102426-Monosaccharides,
pubmed-meshheading:5102426-Neuraminic Acids,
pubmed-meshheading:5102426-Tritium,
pubmed-meshheading:5102426-Viral Proteins
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pubmed:year |
1971
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pubmed:articleTitle |
Modification of Sindbis virus glycoprotein by host-specified glycosyl transferases.
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pubmed:publicationType |
Journal Article
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