| pubmed-article:790390 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:790390 | lifeskim:mentions | umls-concept:C1262946 | lld:lifeskim |
| pubmed-article:790390 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:790390 | lifeskim:mentions | umls-concept:C1336789 | lld:lifeskim |
| pubmed-article:790390 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:790390 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:790390 | pubmed:dateCreated | 1976-12-30 | lld:pubmed |
| pubmed-article:790390 | pubmed:abstractText | The chimaeric protein repressor-galactosidase, in which fully active lac repressor is covalently linked to the active enzyme beta-galactosidase, was used as a system for probing the quaternary structure of lac repressor. Electron micrographs revealed repressor-galactosidase to be a tetrameric aggregate. When lac repressor, alone, was crosslinked with dimethyl suberimidate, dimers, trimers, tetramers, and oligomers of the protein subunit were produced, whereas crosslinking of the tetrameric repressor-galactosidase resulted in the production of only dimers of the chimaera. Treatment of lac repressor with iodine resulted in the formation of protein dimers; the same result was obtained with repressor-galactosidase. After limited proteolysis of lac repressor, no crosslinking was obtained after treatment with dimethyl suberimidate, whereas iodine still produced a covalent linkage. These results are interpreted as evidence that the lac repressor parts of the tetrameric repressor-galactosidase-chimaera are organized as dimers on the tetrameric-beta-galactosidase core. Because this chimaera has been previously shown to have normal repressor activity [B. Müller-Hill and J. Kania (1974) Nature, 249,561-563], we conclude that lac repressor still is biologically active as a dimeric aggregate. | lld:pubmed |
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| pubmed-article:790390 | pubmed:language | eng | lld:pubmed |
| pubmed-article:790390 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:790390 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:790390 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:790390 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:790390 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:790390 | pubmed:author | pubmed-author:BrownD TDT | lld:pubmed |
| pubmed-article:790390 | pubmed:author | pubmed-author:KaniaJJ | lld:pubmed |
| pubmed-article:790390 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:790390 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:790390 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:790390 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:790390 | pubmed:pagination | 3529-33 | lld:pubmed |
| pubmed-article:790390 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:790390 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:790390 | pubmed:articleTitle | The functional repressor parts of a tetrameric lac repressor-beta-galactosidase chimaera are organized as dimers. | lld:pubmed |
| pubmed-article:790390 | pubmed:publicationType | Journal Article | lld:pubmed |
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