Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:2357374rdf:typepubmed:Citationlld:pubmed
pubmed-article:2357374lifeskim:mentionsumls-concept:C0441833lld:lifeskim
pubmed-article:2357374lifeskim:mentionsumls-concept:C0003250lld:lifeskim
pubmed-article:2357374lifeskim:mentionsumls-concept:C0680730lld:lifeskim
pubmed-article:2357374lifeskim:mentionsumls-concept:C0392756lld:lifeskim
pubmed-article:2357374lifeskim:mentionsumls-concept:C1148554lld:lifeskim
pubmed-article:2357374pubmed:issue5lld:pubmed
pubmed-article:2357374pubmed:dateCreated1990-8-1lld:pubmed
pubmed-article:2357374pubmed:abstractTextReduction of disulfide bonds to sulfhydryl groups for direct radiolabeling of antibodies for immunoscintigraphic and therapeutic applications continues to be of considerable interest. Sensitive spectrophotometric methods have been evaluated that will enable investigators to determine submicrogram quantities of cysteine units produced, for the assurance of controlled reduction. One method, which generates a cysteine-ninhydrin complex (520 nm), has a molar extinction coefficient of 30 250 and can determine 0.04 micrograms/ml cysteine units with an absorbance of 0.01. The method has been applied to determine the quantity of cysteine groups produced by the reduction of an immunoglobin G antibody with five different reducing agents in normal to five times the previously determined optimal molar ratios. The quantities of cysteine units produced from the controlled reduction from 240 micrograms immunoglobin G ranged from 0.073 +/- 0.01 to 1.07 +/- 0.04 micrograms, which were merely 0.54 +/- 0.08% to 7.9 +/- 0.28% of the total available disulfide groups in the protein.lld:pubmed
pubmed-article:2357374pubmed:languageenglld:pubmed
pubmed-article:2357374pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:citationSubsetIMlld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2357374pubmed:statusMEDLINElld:pubmed
pubmed-article:2357374pubmed:monthMaylld:pubmed
pubmed-article:2357374pubmed:issn0736-6205lld:pubmed
pubmed-article:2357374pubmed:authorpubmed-author:ThakurM LMLlld:pubmed
pubmed-article:2357374pubmed:authorpubmed-author:DeFulvioJ DJDlld:pubmed
pubmed-article:2357374pubmed:issnTypePrintlld:pubmed
pubmed-article:2357374pubmed:volume8lld:pubmed
pubmed-article:2357374pubmed:ownerNLMlld:pubmed
pubmed-article:2357374pubmed:authorsCompleteYlld:pubmed
pubmed-article:2357374pubmed:pagination512-6lld:pubmed
pubmed-article:2357374pubmed:dateRevised2003-11-14lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:meshHeadingpubmed-meshheading:2357374-...lld:pubmed
pubmed-article:2357374pubmed:year1990lld:pubmed
pubmed-article:2357374pubmed:articleTitleDetermination of reduced disulfide groups in monoclonal antibodies.lld:pubmed
pubmed-article:2357374pubmed:affiliationThomas Jefferson University.lld:pubmed
pubmed-article:2357374pubmed:publicationTypeJournal Articlelld:pubmed