Preparation and metabolism of 125-sulfobromophthalein

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

doi:10.1016/0009-8981(83)90331-5

Preparation and metabolism of ¹²⁵-sulfobromophthalein

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

Medicine

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	321-327
Number of pages	7
Journal	Clinica Chimica Acta
Volume	128
Issue number	2-3
DOIs	https://doi.org/10.1016/0009-8981(83)90331-5
State	Published - Mar 14 1983

ASJC Scopus subject areas

Biochemistry
Clinical Biochemistry
Biochemistry, medical

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@article{8441121dfcf04b9190bdfef8a47410e2,

title = "Preparation and metabolism of 125-sulfobromophthalein",

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.",

author = "Masanori Hirano and Lorenz Theilmann and Stollman, \{Yacov R.\} and Alexander Sosiak and Wolkoff, \{Allan W.\}",

note = "Funding Information: This work was supported in part by NIH AM-17702.",

year = "1983",

month = mar,

day = "14",

doi = "10.1016/0009-8981(83)90331-5",

language = "English (US)",

volume = "128",

pages = "321--327",

journal = "Clinica Chimica Acta",

issn = "0009-8981",

publisher = "Elsevier B.V.",

number = "2-3",

}

TY - JOUR

T1 - Preparation and metabolism of 125-sulfobromophthalein

AU - Hirano, Masanori

AU - Theilmann, Lorenz

AU - Stollman, Yacov R.

AU - Sosiak, Alexander

AU - Wolkoff, Allan W.

N1 - Funding Information: This work was supported in part by NIH AM-17702.

PY - 1983/3/14

Y1 - 1983/3/14

N2 - 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.

AB - 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.

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U2 - 10.1016/0009-8981(83)90331-5

DO - 10.1016/0009-8981(83)90331-5

M3 - Article

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SN - 0009-8981

VL - 128

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EP - 327

JO - Clinica Chimica Acta

JF - Clinica Chimica Acta

IS - 2-3

ER -

Preparation and metabolism of ¹²⁵-sulfobromophthalein

Abstract

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