| pubmed-article:219248 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:219248 | lifeskim:mentions | umls-concept:C0038975 | lld:lifeskim |
| pubmed-article:219248 | lifeskim:mentions | umls-concept:C0002074 | lld:lifeskim |
| pubmed-article:219248 | lifeskim:mentions | umls-concept:C0003343 | lld:lifeskim |
| pubmed-article:219248 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:219248 | lifeskim:mentions | umls-concept:C1998468 | lld:lifeskim |
| pubmed-article:219248 | lifeskim:mentions | umls-concept:C1705920 | lld:lifeskim |
| pubmed-article:219248 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:219248 | pubmed:dateCreated | 1979-6-29 | lld:pubmed |
| pubmed-article:219248 | pubmed:abstractText | We analyzed large and small species of T-antigen by immunoprecipitation and two-dimensional gel electrophoresis. The T-antigen species were subjected to electrophoresis either directly or after reduction and alkylation with N-ethylmaleimide. Treatment with N-ethylmaleimide improved the resolution of large-T by two-dimensional gel electrophoresis and was a requirement for the resolution of small-t antigen on two dimensional gels. Large-T did not form a discrete protein spot, but rather formed a streak from approximately pH 6.5 to 6.9 on isoelectric focusing gels. Small-t formed a sharp protein spot at approximately pH 7.2 when subjected to electrophoresis under non-equilibrium conditions which extended the pH gradient to include proteins with basic isoelectric points. Treatment with N-ethylmaleimide decreased the mobility of the T-antigen species during sodium dodecyl sulfate gel electrophoresis. We suggest that the apparent increase in molecular weight was due to the association of N-ethylmaleimide with cysteine-rich regions of these proteins. Viable deletion mutants of simian virus 40 which do not induce the synthesis of small-t but product small-t-related polypeptides were used to localize the cysteine-rich region of small-t to between 0.54 and 0.59 on the genetic map of simian virus 40. | lld:pubmed |
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| pubmed-article:219248 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:219248 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:219248 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:219248 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:219248 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:219248 | pubmed:author | pubmed-author:O'FarrellP... | lld:pubmed |
| pubmed-article:219248 | pubmed:author | pubmed-author:CrawfordL VLV | lld:pubmed |
| pubmed-article:219248 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:219248 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:219248 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:219248 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:219248 | pubmed:pagination | 587-96 | lld:pubmed |
| pubmed-article:219248 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:219248 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:219248 | pubmed:articleTitle | Effect of alkylation on the physical properties of simian virus 40 T-antigen species. | lld:pubmed |
| pubmed-article:219248 | pubmed:publicationType | Journal Article | lld:pubmed |
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