Linked Life Data

3677327

Source:http://linkedlifedata.com/resource/pubmed/id/3677327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-1-19
pubmed:abstractText
Specific activity of pyruvate kinase decreases as the age of rat erythrocytes increases in fractions obtained by counter-current distribution in dextran-polyethylene glycol biphasic systems; the enzyme is inhibited by ATP and activated by fructose-1,6-bisphosphate at low phosphoenol pyruvate concentrations. Specific activity does not change in fractions from greater than 95 per cent-rich reticulocytes (anaemic rats); the enzyme is inhibited by ATP but not activated by fructose-1,6-bisphosphate. These results can be explained on the basis of different pyruvate kinase isozymes and suggest that decrease in activity is not affecting regulatory properties during erythrocytes aging.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0263-6484
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
301-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Pyruvate kinase activity and response to allosteric effectors in rat erythrocytes and reticulocytes fractionated by multiple partitioning in aqueous two-phase systems.
pubmed:affiliation
Departamento de Bioquímica y Biologia Molecular, Facultad de Farmacia, Universidad de Alcalá de Henares, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't