pubmed-article:11437597 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C0019944 | lld:lifeskim |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
pubmed-article:11437597 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:11437597 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:11437597 | pubmed:dateCreated | 2001-7-4 | lld:pubmed |
pubmed-article:11437597 | pubmed:abstractText | We have expressed horse cytochrome c in Escherichia coli. The gene was designed with E. coli codon bias and assembled by using a recursive polymerase chain reaction method. The far-ultraviolet and near-ultraviolet/Soret circular dichroism (CD) spectra show that the structure of recombinant horse cytochrome c is the same as that of the authentic protein. CD-detected thermal denaturation studies were used to measure the thermodynamic parameters associated with two-state denaturation. The free energy of denaturation for the recombinant protein is 10.0 +/- 2.3 kcal mol(-1) at pH 4.6 and 25 degrees C, which agrees with the value for the authentic protein. The expression system will help advance our understanding of the roles of cytochrome c in electron transfer, oxidative stress, and apoptosis by allowing the production of protein variants. | lld:pubmed |
pubmed-article:11437597 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11437597 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11437597 | pubmed:language | eng | lld:pubmed |
pubmed-article:11437597 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11437597 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11437597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11437597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11437597 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11437597 | pubmed:month | Jul | lld:pubmed |
pubmed-article:11437597 | pubmed:issn | 1046-5928 | lld:pubmed |
pubmed-article:11437597 | pubmed:author | pubmed-author:LangE HEH | lld:pubmed |
pubmed-article:11437597 | pubmed:author | pubmed-author:PielakG JGJ | lld:pubmed |
pubmed-article:11437597 | pubmed:author | pubmed-author:PatelC NCN | lld:pubmed |
pubmed-article:11437597 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
pubmed-article:11437597 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11437597 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:11437597 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11437597 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11437597 | pubmed:pagination | 220-4 | lld:pubmed |
pubmed-article:11437597 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:11437597 | pubmed:meshHeading | pubmed-meshheading:11437597... | lld:pubmed |
pubmed-article:11437597 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11437597 | pubmed:articleTitle | Characterization of horse cytochrome c expressed in Escherichia coli. | lld:pubmed |
pubmed-article:11437597 | pubmed:affiliation | Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA. | lld:pubmed |
pubmed-article:11437597 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11437597 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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