Linked Life Data

3028466

Source:http://linkedlifedata.com/resource/pubmed/id/3028466

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-4-10
pubmed:abstractText
Human erythrocyte pyrimidine 5'-nucleotidase (P5N) was separated into two subclasses. P5N-I and P5N-II, by DEAE Bio-Gel A column chromatography. Their enzymological properties were studied using five normal subjects and five patients with different P5N deficiencies. Study of the normal subjects showed that P5N-I and P5N-II have distinctive properties, and P5N-II is similar to the 5'-nucleotidase in rat liver cytosol. The P5N-II from the five subjects with this deficiency had normal activity and other normal enzymological properties. However, the P5N-I from these patients had abnormal properties, including reduced activity. These variant enzymes had a high Michaelis constant for substrate cytidine 5'-monophosphate and were heat stable. The optimum pH was shifted towards the acidic side in two patients, towards the basic side in one, and was unchanged in the other two. These results strongly suggest that the main cause of P5N deficiency is an abnormality of P5N-I, probably arising from a structural gene mutation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0007-1048
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-41
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Chromatographic analysis of human erythrocyte pyrimidine 5'-nucleotidase from five patients with pyrimidine 5'-nucleotidase deficiency.
pubmed:publicationType
Journal Article, Case Reports, Research Support, Non-U.S. Gov't