Abstract:
:The sodium dodecyl sulfate (SDS) complex of the major glycoprotein of avian myeloblastosis virus exhibited an anomalously low free electrophoretic mobility compared with those of non-glycosylated protein standards. The apparent molecular weight of the glycoprotein calculated from the relation between log molecular weight and electrophoretic mobility depended on the acrylamide concentration and reached a lower limit of 80,000. The molecular weight was also estimated from the retardation coefficients of protein standards and the viral glycoprotein. This method yielded a molecular weight of 64,000 for the avian myeloblastosis virus glycoprotein. When gel chromatography in SDS was used to determine the apparent molecular weight of the glycoprotein from its hydrodynamic properties alone, the estimated value was 50,000. The generally assigned value of 80,000 daltons for the avian myeloblastosis virus major glycoprotein, as determined by SDS electrophoresis, may be an overestimate due to its relatively low free electrophoretic mobility and peculiar conformation in SDS.
journal_name
J Viroljournal_title
Journal of virologyauthors
Marciani DJ,Papamatheakis JDdoi
10.1128/JVI.26.3.825-827.1978subject
Has Abstractpub_date
1978-06-01 00:00:00pages
825-7issue
3eissn
0022-538Xissn
1098-5514journal_volume
26pub_type
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Journal of virology
pub_type: 杂志文章
doi:10.1128/JVI.02337-10
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pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Journal of virology
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pub_type: 杂志文章
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更新日期:2003-03-01 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of virology
pub_type: 杂志文章
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更新日期:1986-03-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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journal_title:Journal of virology
pub_type: 杂志文章
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更新日期:1972-02-01 00:00:00
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pub_type: 杂志文章
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