Binding of taxol to human plasma, albumin and α1-acid glycoprotein

G. N. Kumar, U. K. Walle, K. N. Bhalla, T. Walle

Research output: Contribution to journalArticlepeer-review

116 Scopus citations


The binding of taxol to human plasma and to individual plasma proteins was studied by equilibrium dialysis. Taxol was found to bind extensively (about 95%) without a significant difference between healthy volunteers and cancer patients. At clinically relevant concentrations (0.1 - 6 μM), the binding was found to be concentration independent, indicating nonspecific hydrophobic binding. Human serum albumin and α1-acid glycoprotein were found to contribute about equally to the binding, with a minor contribution from lipoproteins. None of the drugs commonly coadministered with taxol (dexamethasone, diphenhydramine, ranitidine, doxorubicin, 5-fluorouracil and cisplatin) altered the binding of taxol significantly. The protein binding of taxol was found to dramatically decrease the red blood cell uptake of taxol.

Original languageEnglish (US)
Pages (from-to)337-344
Number of pages8
JournalResearch Communications in Chemical Pathology and Pharmacology
Issue number3
StatePublished - 1993

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Toxicology
  • Pharmacology
  • Pharmacology, Toxicology and Pharmaceutics(all)


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