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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 3
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pubmed:dateCreated |
1983-10-28
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pubmed:abstractText |
The mutant forms of uridylyl transferase of eight galactosemic patients and two 'Rennes' variants were characterized with regard to the presence and level of immunoreactive protein, the apparent subunit molecular weight and the isoelectric point. Semi-purified haemolysates were studied by various electrophoretic techniques, then proteins were electrophoretically transferred on to nitrocellulose filters. They were treated with specific anti-transferase antibodies, and then with radioiodinated protein A, followed by autoradiography. We have found that: in all cases, a cross-reacting material was detectable, with a molecular subunit size of 46 000, indistinguishable from that of controls. a biochemical heterogeneity of the mutant enzyme was found: the amount of apparent immunologically reactive protein varied from 20 to 100% of that of controls; electrophoretic experiments performed on two 'Rennes' variants showed an increased negative charge.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0003-4800
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
177-85
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6311074-Adolescent,
pubmed-meshheading:6311074-Adult,
pubmed-meshheading:6311074-Child,
pubmed-meshheading:6311074-Child, Preschool,
pubmed-meshheading:6311074-Cross Reactions,
pubmed-meshheading:6311074-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6311074-Galactosemias,
pubmed-meshheading:6311074-Genetic Variation,
pubmed-meshheading:6311074-Humans,
pubmed-meshheading:6311074-Isoelectric Focusing,
pubmed-meshheading:6311074-Molecular Weight,
pubmed-meshheading:6311074-Mutation,
pubmed-meshheading:6311074-Nucleotidyltransferases,
pubmed-meshheading:6311074-UTP-Hexose-1-Phosphate Uridylyltransferase
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pubmed:year |
1983
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pubmed:articleTitle |
Molecular studies on galactose 1 phosphate uridylyl transferase from normal and mutant subjects. An immunological approach.
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pubmed:publicationType |
Journal Article
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