Stereoselective binding of tertatolol and of 4-hydroxytertatolol to human plasma proteins.
The binding of racemic tertatolol and 4-hydroxytertatolol and of their enantiomers was compared in alpha 1-acid glycoprotein and albumin solutions. The binding rate of S(-)tertatolol to alpha 1-acid glycoprotein was much greater than that of R(+)tertatolol, the binding of the racemate being intermediate. It was the reverse for the binding to albumin, although the differences were slight. The binding of 4-hydroxytertatolol racemate and enantiomers was very low as compared to the binding of tertatolol, and there were no statistically significant differences in the binding of the 4-hydroxytertatolol enantiomers to either alpha 1-acid glycoprotein or albumin.
Bastian
G
G
INSERM, Paris, France.
Urien
S
S
Brée
F
F
Jolliet
P
P
Rocher
I
I
Crambes
O
O
Tillement
J P
JP
D000319:Adrenergic beta-Antagonists / Q000097:blood*; D001665:Binding Sites; D001798:Blood Proteins / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009961:Orosomucoid / Q000378:metabolism; D011412:Propanolamines / Q000097:blood*; D012709:Serum Albumin / Q000378:metabolism; D013237:Stereoisomerism; D013876:Thiophenes
D000319:Adrenergic beta-Antagonists; D001798:Blood Proteins; D009961:Orosomucoid; D011412:Propanolamines; D012709:Serum Albumin; D013876:Thiophenes; C054865:4-hydroxytertatolol; C005632:tertatolol