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Lactosylation of albumin reduces uptake rate of dibromosulfophthalein in perfused rat liver and dissociation rate from albuminIn Vitro by Peter Van Der Sluijs; Bart Postema; Dirk K. F. Meijer is a Medicine article available to read on EtoBox.

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Two types of models have recently been proposed to describe hepatic uptake kinetics of protein bound drugs: a model in which dissociation from plasma protein is rate limiting the process, and a model in which an interaction between protein and hepatocyte surface is thought to promote dissociation and uptake of the drug. This study was designed to investigate several aspects of both models, using lactosylated albumin as a binding protein that can interact with the Ashwell receptor abundantly present on the hepatocyte. Dibromosulfophthalein clearance was studied in rat liver in the presence of 150 p M ( 1 %) albumin or 150 pM lactosylated albumin. Initial disappearance rate from perfusate in the presence of lactosylated albumin indicated a 2-fold decrease in hepatic uptake rate compared with native albumin. This was confirmed by compartmental analysis, showing a similar decrease in hepatic uptake rate constant. Protein binding of dibromosulfophthalein to lactosylated albumin was only marginally different from normal albumin. Consequently, modification of the protein retarded uptake of the organic anion at an essentially unchanged unbound concentration. Fluorescence spectroscopy of la

Who reads Lactosylation of albumin reduces uptake rate of dibromosulfophthalein in perfused rat liver and dissociation rate from albuminIn Vitro?

Author

Peter Van Der Sluijs; Bart Postema; Dirk K. F. Meijer

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Elsevier BV; Wiley; Research Square (ISSN 0270-9139)

Published

1987

Language

EN

Field

Medicine (Health Sciences)