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The binding of prednisolone in human serum and to recrystallized human albumin in vitro.
Author(s) -
Steele WH,
Hawksworth GM,
Barber HE
Publication year - 1982
Publication title -
british journal of clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.216
H-Index - 146
eISSN - 1365-2125
pISSN - 0306-5251
DOI - 10.1111/j.1365-2125.1982.tb04954.x
Subject(s) - transcortin , prednisolone , albumin , plasma protein binding , ultrafiltration (renal) , serum albumin , human serum albumin , binding site , chemistry , endocrinology , blood proteins , medicine , globulin , chromatography , biochemistry
1 Prednisolone binding in human serum and to recrystallized human serum albumin was measured by continuous ultrafiltration. 2 At serum concentrations of prednisolone up to 0.6 micron, 95.0% was bound but at higher concentrations the binding became non‐linear falling to 80.5% at 1.8 microns. At even higher concentrations binding in serum became linear again and paralleled the binding to albumin which was linear throughout the entire range of prednisolone concentrations. 3 A binding model was proposed which included a saturable component attributable to binding to transcortin and a non‐saturable binding to albumin. 4 Computer simulations using the experimentally determined binding parameters of the model indicated that binding in serum was critically dependent on transcortin concentration and almost independent of albumin concentration.