| pubmed-article:8144534 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8144534 | lifeskim:mentions | umls-concept:C0035286 | lld:lifeskim |
| pubmed-article:8144534 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8144534 | lifeskim:mentions | umls-concept:C1881488 | lld:lifeskim |
| pubmed-article:8144534 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8144534 | pubmed:dateCreated | 1994-5-5 | lld:pubmed |
| pubmed-article:8144534 | pubmed:abstractText | We have developed an assay for chaperone-mediated protein renaturation using thermally denatured Firefly luciferase. Dilution of denatured luciferase (> 99% loss of activity) into reticulocyte lysate typically results in recovery of 5-15% activity. Addition of an ATP-regenerating system increases yields to > 60%, while heat shock or the addition of denatured proteins inhibits the chaperoning activity. Reticulocyte lysate contains abundant quantities of the heat shock proteins, hsp90 and hsp70, and a 60-kDa protein homologous to the yeast stress protein, STI1. Immune isolated samples of these three proteins support recovery of up to 35% of luciferase activity in an ATP-dependent manner, suggesting that these or associated proteins are involved in the renaturation of luciferase. Furthermore, we observed a correlation between luciferase renaturation activity and the levels of hsp70 and hsp90 in reticulocyte lysate preparations. Purified hsp90 and hsp70, along with an ATP-regenerating system, are able to renature luciferase to greater than 20% of its original activity. This renaturation is most efficient when hsp90 and hsp70 are at about a 2:1 ratio and at concentrations similar to those found in reticulocyte lysate. This study provides evidence for an ATP-dependent chaperoning activity in reticulocyte lysate that involves a cooperative action of hsp70 and hsp90. | lld:pubmed |
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| pubmed-article:8144534 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8144534 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8144534 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8144534 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8144534 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8144534 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8144534 | pubmed:author | pubmed-author:ToftD ODO | lld:pubmed |
| pubmed-article:8144534 | pubmed:author | pubmed-author:HurthMM | lld:pubmed |
| pubmed-article:8144534 | pubmed:author | pubmed-author:MattsR LRL | lld:pubmed |
| pubmed-article:8144534 | pubmed:author | pubmed-author:McMahonN JNJ | lld:pubmed |
| pubmed-article:8144534 | pubmed:author | pubmed-author:SullivanW PWP | lld:pubmed |
| pubmed-article:8144534 | pubmed:author | pubmed-author:SchumacherR... | lld:pubmed |
| pubmed-article:8144534 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8144534 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8144534 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8144534 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8144534 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8144534 | pubmed:pagination | 9493-9 | lld:pubmed |
| pubmed-article:8144534 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8144534 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8144534 | pubmed:articleTitle | ATP-dependent chaperoning activity of reticulocyte lysate. | lld:pubmed |
| pubmed-article:8144534 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Mayo Graduate School, Rochester, Minnesota 55905. | lld:pubmed |
| pubmed-article:8144534 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8144534 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8144534 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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