Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
1983-10-28
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-4800
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Molecular studies on galactose 1 phosphate uridylyl transferase from normal and mutant subjects. An immunological approach.
pubmed:publicationType
Journal Article