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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.
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