Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1979-6-11
pubmed:abstractText
Phosphoenolpyruvate carboxykinase has been purified by a procedure involving chromatography on norleucine-Sepharose, using a decreasing (NH4)2 SO4-inorganic phosphate concentration gradient, followed by chromatography on GMP-Sepharose. The enzyme is eluted from the affinity column with 2.5 X 10(-5)m IDP. The same procedure is applicable to hog mitochondrial and cytosol enzymes yielding the enzyme as a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The corresponding molecular weight is 65,000 for each enzyme. Discontinuous polyacrylamide gel electrophoresis of the mitochondrial enzyme gave two sharp bands that were found to contain carboxykinase activity upon assay of gel slices. Similar analysis of the cytosol enzyme showed a much different staining pattern and four regions of carboxykinase activity. Plots of relative mobility of the two mitochondrial bands vs. per cent polyacrylamide in the gels gave parallel lines, confirming that the two bands did not result from enzyme aggregation. Elution of the enzyme upon analytical Sephacryl S-200 chromatography did, however, produce some resolution of the two bands without change in specific activity. The purification procedure described above has been applied also to the human mitochondrial enzyme with similar results. The molecular weight, similarly is 68,000.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0032-7484
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Purification of hepatic phosphoenolpyruvate carboxykinase by affinity and hydrophobic chromatography.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.