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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
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pubmed:dateCreated |
1978-9-29
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pubmed:abstractText |
Pyruvate kinase deficiency was found to be the causative factor in a family with nonspherocytic hemolytic anemia. Biochemical findings were the following: decrease in adenosine-5'-triphosphate (ATP) concentration (59 micromoles per 100 ml of erytrocytes; normal: 150 +/- 59), increase in 2,3-diphosphoglycerate (2,3-DPG) concentration (13611 micromoles per 100 ml of erythrocytes; normal: 480 +/- 80) and low level of pyruvate kinase activity (955 U) mmol Hb; normal 2700 +/- 498. The deficiency of enzyme activity in the hexose-monophosphate shunt was excluded on bases of normal or elevated glucose-6-phosphate and 6-phosphogluconate dehydrogenase activities, normal reduced glutathione concentration and normal glutathione stability in vitro. The Michaelis constant for phosphoenolpyruvate of the patient's pyruvate kinase was found to be normal; thus, the mutation affected only the Vmax of the enzyme.
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pubmed:language |
hrv
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0350-2023
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
95-6
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pubmed:dateRevised |
2009-11-9
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pubmed:meshHeading | |
pubmed:year |
1977
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pubmed:articleTitle |
[Deficiency of pyruvate kinase in erythrocytes: biochemical studies. Preliminary communication].
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pubmed:publicationType |
Journal Article,
English Abstract,
Case Reports
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