Linked Life Data

219973

Source:http://linkedlifedata.com/resource/pubmed/id/219973

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-7-16
pubmed:abstractText
A neutral, membrane-bound, phosphatase activity was characterized in normal red blood cells, using p-nitrophenylphosphate as substrate. Its specific activity was 1.59 nmol mg-1 min-1. The kinetics were of the Michaelis type: KM,app = 2.5 X 10(-3) M. It was stimulated by K+ and inhibited by ouabain, a behaviour reminiscent of (Na+ + K+)-ATPase. In 10 patients with homozygous sickle cell disease and in 11 patients with unidentified congenital hemolytic anemias, the specific activity was significantly increased. In general, the phosphatase retained Michaelis-Menten kinetics. However, in four patients from the same family with an unidentified hemolytic anemia, the kinetics yielded a biphasic curve instead of a rectangular hyperbola, a change consistent with the existence of an inhibition by substrate excess. From detailed analysis of the curve, the apparent inhibitor constant for pNPP was determined: Ki,app approx. 2.5 X 10(-2) M. This novel abnormality of the red cell membrane might be the distinctive feature of a given type of congenital hemolytic anemia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-24
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Properties of a membrane-bound phosphatase activity in normal and abnormal red blood cells.
pubmed:publicationType
Journal Article