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PubMed · 7082362

Erythromycin binding to human serum.

G A Dette·H Knothe·G Herrmann
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Abstract

Erythromycin binding to human serum was measured under conditions of binding equilibrium. The binding is sensitive to pH changes, decreasing at acid pH. Over a great range of serum dilution, the bound fraction is semilogarithmically related to serum concentration. Binding is shown to be completely reversible. With increasing erythromycin concentration a specific part of binding is saturable and specifically displaceable by erythromycin is specifically bound to a single class of noninteracting binding sites with an apparent dissociation constant Kd = 5.9 microM (38 degrees C). The kinetic and thermodynamic parameters at 25 degrees are: Kd = 8.4 microM, delta H degrees = +4.4 X 10(3) cal per mole, delta G degrees = 6.9 X 10(3) cal per mole, delta S degrees = +38 e.u.

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Blood ProteinsErythromycinHumansHydrogen-Ion ConcentrationKineticsProtein BindingTemperatureJournal Article

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G A Dette, H Knothe, G Herrmann. 1982-03-15. Erythromycin binding to human serum.. https://doi.org/10.1016/0006-2952(82)90346-x

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