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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1989-10-23
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pubmed:abstractText |
Crude barium chloride eluates prepared from 12 unrelated patients with cross-reacting material positive (CRM+) haemophilia B were activated with celite eluate, the reaction products resolved after reduction by 13% SDS-PAGE, and factor IX antigenic material detected by probing with radiolabelled immunopurified rabbit anti-factor IX antiserum followed by autoradiography. Out of the 12, one sample showed faulty activation with the production of a stable reaction product with a MW compatible with that of a putative light chain-activation intermediate. In order to confirm this, two oligonucleotide primers that bracketed exon 6 of the factor IX gene were constructed and used to prime a polymerase chain reaction on DNA isolated from the patient's peripheral blood leucocytes. A single 489 nucleotide DNA fragment was obtained, gel purified, subcloned into M13, and DNA sequencing carried out on both strands. A single C to T transition was discovered that changed the Arg residue at position 145, the first residue of the first bond in the activation peptide, to a Cys, a result that confirmed the inferences drawn from the activation studies.
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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 |
Aug
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pubmed:issn |
0007-1048
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
556-60
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2775660-Antigens,
pubmed-meshheading:2775660-Arginine,
pubmed-meshheading:2775660-Base Sequence,
pubmed-meshheading:2775660-Cloning, Molecular,
pubmed-meshheading:2775660-Cysteine,
pubmed-meshheading:2775660-DNA,
pubmed-meshheading:2775660-Exons,
pubmed-meshheading:2775660-Factor IX,
pubmed-meshheading:2775660-Gene Expression Regulation,
pubmed-meshheading:2775660-Hemophilia B,
pubmed-meshheading:2775660-Humans,
pubmed-meshheading:2775660-Molecular Weight
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pubmed:year |
1989
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pubmed:articleTitle |
Factor IX Cardiff: a variant factor IX protein that shows abnormal activation is caused by an arginine to cysteine substitution at position 145.
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pubmed:affiliation |
Department of Haematology, University of Wales College of Medicine, Cardiff, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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