Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-4-16
pubmed:abstractText
Kinetic studies were carried out on pyruvate kinase and phosphofructokinase from the lizard Lacerta galloti. Pyruvate kinase is inhibited by ATP and activated by fructose 1,6-biphosphate giving an hyperbolic saturation curve for ATP without the activator which becomes sigmoidal at saturating concentrations of fructose 1,6-biphosphate, giving a moderate cooperativity with a Hill coefficient of h = 1.72. Binding of fructose 1,6-biphosphate to pyruvate kinase was studied as protection effect against thermal denaturation, this being the most suitable ligand tested to avoid the loss of activity. Phosphofructokinase is inhibited by ATP at millimolar range and activated by AMP and by fructose 2,6-biphosphate, AMP being the more efficient activator.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
289-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Regulation of glycolysis in lizards: kinetic studies on liver pyruvate kinase and phosphofructokinase from Lacerta galloti.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't