| pubmed-article:8401214 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8401214 | lifeskim:mentions | umls-concept:C0021760 | lld:lifeskim |
| pubmed-article:8401214 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8401214 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:8401214 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:8401214 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:8401214 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8401214 | pubmed:dateCreated | 1993-10-28 | lld:pubmed |
| pubmed-article:8401214 | pubmed:abstractText | The conformation and stability of a recombinant mouse interleukin-6 (mIL-6) has been investigated by analytical ultracentrifugation, fluorescence spectroscopy, urea-gradient gel electrophoresis, and near- and far-ultraviolet circular dichroism. On decreasing the pH from 8.0 to 4.0, the tryptophan fluorescence of mIL-6 was quenched 40%, the midpoint of the transition occurring at pH 6.9. The change in fluorescence quantum yield was not due to unfolding of the molecule because the conformation of mIL-6, as judged by both urea-gradient gel electrophoresis and CD spectroscopy, was stable over the pH range 2.0-10.0. Sedimentation equilibrium experiments indicated that mIL-6 was monomeric, with a molecular mass of 22,500 Da over the pH range used in these physicochemical studies. Quenching of tryptophan fluorescence (20%) also occurred in the presence of 6 M guanidine hydrochloride upon going from pH 7.4 to 4.0 suggesting that an amino acid residue vicinal in the primary structure to one or both of the two tryptophan residues, Trp-36 and Trp-160, may be partially involved in the quenching of endogenous fluorescence. In this regard, similar results were obtained for a 17-residue synthetic peptide, peptide H1, which corresponds to an N-terminal region of mIL-6 (residues Val-27-Lys-43). The pH-dependent acid quenching of endogenous tryptophan fluorescence of peptide H1 was 30% in the random coil conformation and 60% in the presence of alpha-helix-promoting solvents. Replacement of His-33 with Ala-33 in peptide H1 alleviated a significant portion of the pH-dependent quenching of fluorescence suggesting that the interaction of the imidazole ring of His-33 with the indole ring of Trp-36 is a major determinant responsible for the quenching of the endogenous protein fluorescence of mIL-6. | lld:pubmed |
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| pubmed-article:8401214 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8401214 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8401214 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8401214 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8401214 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8401214 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:8401214 | pubmed:author | pubmed-author:SimpsonR JRJ | lld:pubmed |
| pubmed-article:8401214 | pubmed:author | pubmed-author:PrestonBB | lld:pubmed |
| pubmed-article:8401214 | pubmed:author | pubmed-author:ZhangJ GJG | lld:pubmed |
| pubmed-article:8401214 | pubmed:author | pubmed-author:WardL DLD | lld:pubmed |
| pubmed-article:8401214 | pubmed:author | pubmed-author:CheckleyGG | lld:pubmed |
| pubmed-article:8401214 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8401214 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:8401214 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8401214 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8401214 | pubmed:pagination | 1291-300 | lld:pubmed |
| pubmed-article:8401214 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8401214 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8401214 | pubmed:articleTitle | Effect of pH and denaturants on the folding and stability of murine interleukin-6. | lld:pubmed |
| pubmed-article:8401214 | pubmed:affiliation | Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Parkville, Victoria, Australia. | lld:pubmed |
| pubmed-article:8401214 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8401214 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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