| Autor: |
Demant EJ; Department of Medical Biochemistry and Genetics, Biochemistry Laboratory C, The Panum Institute, University of Copenhagen, Denmark., Friche E |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical pharmacology [Biochem Pharmacol] 1998 Jan 01; Vol. 55 (1), pp. 27-32. |
| DOI: |
10.1016/s0006-2952(97)00437-1 |
| Abstrakt: |
A Sephadex G-200 gel filtration method was used to measure directly the equilibrium binding of five important anthracycline analogs to serum albumin. The order of the overall binding constant (K) in a 150 mM NaCl, 20 mM Hepes buffer (pH 7.45) was doxorubicin < daunorubicin < 4-demethoxydaunorubicin approximately 13-dihydro-4'-deoxy-4'-iododoxorubicin < 4'-deoxy-4'-iododoxorubicin for human serum albumin (K = 2.67 +/- 0.07 mM(-1) to 24.5 +/- 3.1 mM[-1]) and bovine serum albumin (K = 1.36 +/- 0.25 mM(-1) to 48.4 +/- 5.2 mM[-1]). Data were given on the pH-dependence of K. The anthracycline-albumin association reaction was compared with measurements of drug partitioning into unilamellar phospholipid membranes and octanol. The results provide important new data required for a systematic kinetic analysis of anthracycline transport in tumor cells under serum conditions in a biological system. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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