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
C2 - 6851140
AN - SCOPUS:0020645589
SN - 0009-8981
VL - 128
SP - 321
EP - 327
JO - Clinica Chimica Acta
JF - Clinica Chimica Acta
IS - 2-3
ER -