Preparation and metabolism of 125-sulfobromophthalein

Masanori Hirano, Lorenz Theilmann, Yacov R. Stollman, Alexander Sosiak, Allan W. Wolkoff

Research output: Contribution to journalArticle

Abstract

Metabolism of 125I-sulfobromophthalein (BSP) prepared by the chloramine-T method was studied in rats. 125I-BSP is removed rapidly from the circulation. However, as compared to BSP, its plasma clearance and biliary excretion are delayed, and its accumulation in the liver is prolonged. Although BSP and 125I-BSP show similar binding to albumin in serum, their binding properties to liver cytosolic proteins and to the liver cell plasma membrane organic anion binding protein (OABP) differ. In contrast to the X-, Y- and Z-protein binding of BSP, 125I-BSP binds predominantly to a high molecular weight protein and only a small proportion of 125I-BSP binds to OABP.

Original languageEnglish (US)
Pages (from-to)321-327
Number of pages7
JournalClinica Chimica Acta
Volume128
Issue number2-3
DOIs
StatePublished - Mar 14 1983

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Biochemistry, medical

Fingerprint Dive into the research topics of 'Preparation and metabolism of <sup>125</sup>-sulfobromophthalein'. Together they form a unique fingerprint.

  • Cite this