The binding of sulfaphenazole to fetal, neonatal, and adult human plasma albumin

Colin F. Chignell, Elliot S. Vesell, Donnas K. Starkweather, Cheston M. Berlin

Research output: Contribution to journalArticle

37 Scopus citations

Abstract

In man, sul f aphenazole has a lower affinity for the albumin o f the fetus and neonate than for that of the adult. Removal of bound endogenous anions from neonatal albumin by treatment with charcoal at pH 3.0 restored the affinity of the protein for sulfaphenazole to the adult level. Prior treatment of adult albumin with bilirubin reduced the affinity of the protein for sulfaphenazole to that observed in fetal and neonatal albumins. Thus the reduced affinity of sulfaphenazole for fetal and neonatal albumin compared to that for adult albumin probably is the result o f the presence o f a tightly bound endogenous ligand, such as bilirubin, on fetal and neonatal albumin.

Original languageEnglish (US)
Pages (from-to)897-901
Number of pages5
JournalClinical pharmacology and therapeutics
Volume12
Issue number6
DOIs
StatePublished - Jan 1 1971

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmacology (medical)

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