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Article (Scientific journals)
Role de l' alpha 1-glycoproteine acide plasmatique dans la fixation de l'aminopyrine.
El Allaf, Dia; Demey-Ponsart, E.; Pirotte, J. et al.
1986In Archives Internationales de Physiologie et de Biochimie, 94 (5), p. 317-22
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Keywords :
Aminopyrine/blood; Binding Sites; Humans; Myocardial Infarction/blood; Orosomucoid/blood; Protein Binding
Abstract :
[en] Under certain pathological conditions the binding of various substances by serum proteins is altered. The plasma concentrations of alpha 1-acid glycoprotein, also known as orosomucoid are reported to be elevated in stressful situation and in certain disease states like acute myocardial infarction. The binding of aminopyrine to serum proteins and alpha 1-acid glycoprotein was determined using equilibrium dialysis. It appears that alpha 1-acid glycoprotein has specific binding sites for aminopyrine. Aminopyrine was also bound to other serum proteins. On addition the results indicate that an increase of alpha 1-acid glycoprotein to concentrations such as those seen in some pathological states does not really alter the percent of aminopyrine bind to serum proteins.
Disciplines :
Laboratory medicine & medical technology
Author, co-author :
El Allaf, Dia ;  Centre Hospitalier Universitaire de Liège - CHU > Cardiologie
Demey-Ponsart, E.
Pirotte, J.
Chapelle, Jean-Paul ;  Université de Liège - ULiège > Département de pharmacie > Chimie médicale
el Allaf, M.
Carlier, J.
Van Cauwenberge, Henry;  Centre Hospitalier Universitaire de Liège - CHU > Chirurgie appareil locomoteur
Language :
French
Title :
Role de l' alpha 1-glycoproteine acide plasmatique dans la fixation de l'aminopyrine.
Alternative titles :
[en] The role of plasma alpha 1-glycoprotein acid in the binding of aminopyrine
Publication date :
1986
Journal title :
Archives Internationales de Physiologie et de Biochimie
ISSN :
0003-9799
Publisher :
Vaillant Carmanne, Liège, Belgium
Volume :
94
Issue :
5
Pages :
317-22
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 23 February 2010

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