CORTISOL-BINDING PROTEIN IN THE CYTOSOL OF RAT CARRAGEENIN GRANULOMA

概要

論文の詳細を見る
Cortisol-binding protein was prepared and partially purified by (NH4)2SO4 fractionation and DEAE-cellulose column chromatography from 105, 000 g supernatant fraction of cytoplasm in rat carrageenin granuloma, which is assumed to be one of the most appropriate experimental models of inflammation. The cortisol-binding protein in the inflammatous tissue, although similar to transcortine, was not transcortine itself. The binding protein was eluted at 0.12 M NaCl by DEAE-cellulose column chromatography with a shallow salt gradient. Sedimentation constant and dissociation constant of the binding protein were 4-5 S and 1.0×10-9 M, respectively. Optimum pH for binding to cortisol was 8.0. Binding ability of the binding protein to cortisol was very sensitive to pronase E and trypsin but resistant to RNase. Specificity of the protein for binding other steroids revealed that 17β-estradiol did not bind to the protein, while androstenedione and testosterone had one sixth as much affinity to the binding protein as that of cortisol. There was good a correlation between the amount of the binding protein in the inflammatory tissue and anti-inflammatory effect of cortisol. Namely, the maximum cortisol-binding ability was seen on a 5 day old granuloma which is the so called `steroid sensitive stage. Thereafter, the binding ability decreased with the increasing stage of granuloma.
社団法人日本薬理学会の論文