Linked Life Data

6442908

Source:http://linkedlifedata.com/resource/pubmed/id/6442908

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1985-7-10
pubmed:abstractText
Five commercial factor VIII (FVIII) concentrates and three prothrombin complex concentrates (PCC) were studied with reference to the qualitative evaluation of factors II, IX, fibronectin, alpha 2-antiplasmin (alpha 2-AP), antithrombin III (AT-III) and subunits A and S of FXIII by crossed-immunoelectrophoresis (CIE) and von Willebrand factor antigen (vWF:Ag) by radio-CIE. This latter protein had a different pattern with the absence or a decrease of larger forms and the presence of a fast-moving precipitating peak, suggesting degradation of the vWF:Ag in FVIII concentrates. In contrast, the electrophoretic mobility of fibronectin, alpha 2-AP and AT-III was normal. All PCC showed a more anodic mobility of factor IX. alpha 2-AP also exhibited a different electrophoretic pattern to that of normal plasma. Abnormality of AT-III was also found in heparin-binding studies. The techniques used in the purification procedures are probably the mechanism responsible for the partial denaturing of these proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-0147
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
453-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Coagulation proteins showing abnormal electrophoretic mobility in commercial concentrates of factor VIII and prothrombin complex.
pubmed:publicationType
Journal Article, Comparative Study