Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:8620065rdf:typepubmed:Citationlld:pubmed
pubmed-article:8620065lifeskim:mentionsumls-concept:C0205474lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C0229982lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C0229671lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C0022920lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C0449416lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C0034378lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C2603343lld:lifeskim
pubmed-article:8620065lifeskim:mentionsumls-concept:C0680536lld:lifeskim
pubmed-article:8620065pubmed:issue11lld:pubmed
pubmed-article:8620065pubmed:dateCreated1996-6-14lld:pubmed
pubmed-article:8620065pubmed:abstractTextWe assayed the isoenzymes of lactate dehydrogenase (EC 1.1.1.27) in commercial quality control sea and several animal tissue extracts, using electrophoresis. We compared the Km values and activation energies of the isoenzymes, in order to find suitable animal tissue sources with a similar isoenzyme profile to that of human serum lactate dehydrogenase. Some of the control sera contained only one isoenzyme fraction corresponding to porcine heart isoenzyme-1 or chicken heart isoenzyme-1, which showed essentially no changes of enzyme activity as a function of pyruvate substrate concentration. Other control sera, which contained isoenzymes from human red cells haemolysates, or from animal tissue extracts with a human serum matrix, showed significant changes of enzyme activity was a function of substrate concentration, and showed different Km values and activation energies from those of human serum. Of the serum and tissue samples from several animal sources, rat heart and kidney extracts showed the greatest similarity to human serum, with respect to the electrophoretic pattern and the Km, pH optimum and activation energy of lactate dehydrogenase isoenzymes.lld:pubmed
pubmed-article:8620065pubmed:languageenglld:pubmed
pubmed-article:8620065pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8620065pubmed:citationSubsetIMlld:pubmed
pubmed-article:8620065pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8620065pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8620065pubmed:statusMEDLINElld:pubmed
pubmed-article:8620065pubmed:monthNovlld:pubmed
pubmed-article:8620065pubmed:issn0939-4974lld:pubmed
pubmed-article:8620065pubmed:authorpubmed-author:YoshidaHHlld:pubmed
pubmed-article:8620065pubmed:authorpubmed-author:YamamotoRRlld:pubmed
pubmed-article:8620065pubmed:authorpubmed-author:HayR LRLlld:pubmed
pubmed-article:8620065pubmed:authorpubmed-author:TanishimaKKlld:pubmed
pubmed-article:8620065pubmed:issnTypePrintlld:pubmed
pubmed-article:8620065pubmed:volume33lld:pubmed
pubmed-article:8620065pubmed:ownerNLMlld:pubmed
pubmed-article:8620065pubmed:authorsCompleteYlld:pubmed
pubmed-article:8620065pubmed:pagination865-8lld:pubmed
pubmed-article:8620065pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:meshHeadingpubmed-meshheading:8620065-...lld:pubmed
pubmed-article:8620065pubmed:year1995lld:pubmed
pubmed-article:8620065pubmed:articleTitleBiochemical and enzymological study of lactate dehydrogenase isoenzymes from commercial quality control sera and several animal tissue sources.lld:pubmed
pubmed-article:8620065pubmed:affiliationDepartment of Clinical Laboratory Sciences, School of Allied Medical Professions, Kanazawa University, Ishikawa, Japan.lld:pubmed
pubmed-article:8620065pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8620065pubmed:publicationTypeComparative Studylld:pubmed