PMID- 6584879
OWN - NLM
STAT- MEDLINE
DCOM- 19840511
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 80
IP  - 24
DP  - 1983 Dec
TI  - Plasma clearance of sulfobromophthalein and its interaction with hepatic binding 
      proteins in normal and analbuminemic rats: is plasma albumin essential for 
      vectorial transport of organic anions in the liver?
PG  - 7654-8
AB  - To investigate a possible function of plasma albumin in the vectorial transport 
      of organic anions by the liver, the plasma disappearance of sulfobromophthalein 
      (BSP) and its interaction with plasma and liver cytosolic proteins were studied 
      in normal rats and mutant Nagase analbuminemic rats (NAR). After intravenous 
      administration of BSP, plasma BSP decreased rapidly in both NAR and control 
      animals: plasma clearance values of BSP in NAR and controls were 12.45 and 7.40 
      ml/min per kg, respectively. Gel exclusion Sephadex G-100 chromatography of BSP 
      with control rat serum revealed a protein peak in the void volume and another in 
      the albumin fraction. BSP chromatographed exclusively with the albumin fraction; 
      binding of BSP to plasma albumin occurred stoichiometrically. Similar studies 
      with NAR serum revealed a single protein peak, in the void volume; a small amount 
      of BSP chromatographed with this protein peak. The amount of BSP that 
      chromatographed with NAR serum protein(s) was 8% of that with control rat serum 
      albumin. Sephadex G-100 chromatography of BSP with control rat liver cytosol 
      revealed four peaks of protein-bound BSP in fractions corresponding to the void 
      volume (fraction X), albumin, glutathione S-transferases (fraction Y, Mr 45,000), 
      and fraction Z (Mr 12,000); fraction Y was the major component of BSP binding. 
      Gel chromatography of NAR liver cytosol with BSP revealed three BSP peaks, 
      fractions X, Y, and Z; fraction X was the major component of BSP binding. Total 
      BSP binding by 30 mg of hepatic cytosolic proteins was 4.5 nmol for controls and 
      10.4 nmol for NAR. Isoelectric focusing of liver cytosol revealed no quantitative 
      or qualitative differences in glutathione S-transferase isozymes between control 
      and mutant animals. Intravenously administered BSP (5 mumol/kg) rapidly appeared 
      in bile as the free form and the glutathione conjugate in normal rats and NAR; 
      41% and 57% of injected BSP was excreted within 60 min in NAR and control rat 
      bile, respectively. These results indicate that binding of BSP to plasma albumin 
      is not indispensable to transhepatocyte transport of BSP in vivo.
FAU - Inoue, M
AU  - Inoue M
FAU - Okajima, K
AU  - Okajima K
FAU - Nagase, S
AU  - Nagase S
FAU - Morino, Y
AU  - Morino Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Blood Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Serum Albumin)
RN  - 0C2P5QKL36 (Sulfobromophthalein)
RN  - 52682-84-5 ((sulfobromophthalein)glutathione conjugate)
RN  - EC 2.5.1.18 (Glutathione Transferase)
RN  - GAN16C9B8O (Glutathione)
SB  - IM
MH  - Animals
MH  - Bile/metabolism
MH  - Blood Proteins/metabolism
MH  - Carrier Proteins/*metabolism
MH  - Cytosol/metabolism
MH  - Glutathione/metabolism
MH  - Glutathione Transferase/metabolism
MH  - Kinetics
MH  - Liver/*metabolism
MH  - Male
MH  - Rats
MH  - Rats, Inbred Strains
MH  - Serum Albumin/*deficiency
MH  - Sulfobromophthalein/*blood/metabolism
PMC - PMC534399
EDAT- 1983/12/01 00:00
MHDA- 1983/12/01 00:01
PMCR- 1984/06/01
CRDT- 1983/12/01 00:00
PHST- 1983/12/01 00:00 [pubmed]
PHST- 1983/12/01 00:01 [medline]
PHST- 1983/12/01 00:00 [entrez]
PHST- 1984/06/01 00:00 [pmc-release]
AID - 10.1073/pnas.80.24.7654 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1983 Dec;80(24):7654-8. doi: 10.1073/pnas.80.24.7654.