Nemoto T, Ohara-Nemoto Y, Kurokawa R, Sato M, Ota M
Department of Biochemistry, Iwate Medical University School of Dentistry, Japan.
Biochem Int. 1988 May;16(5):973-81.
The transformed glucocorticoid receptor (GR) from rat liver precipitated at 30% saturation of ammonium sulfate and sedimented at 4.3 S on glycerol gradient centrifugation, whereas the nontransformed GR precipitated at higher concentrations of ammonium sulfate (40-50% saturation) and sedimented at 8.6 S on a gradient. Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that heat shock protein 90 (hsp 90) precipitated at 40-50% saturation of ammonium sulfate. Moreover, hsp 90 and the nontransformed GR were eluted from DEAE high performance ion-exchange chromatography at similar salt concentrations (0.22-0.23 M NaCl), whereas the transformed GR was eluted at 0.1 M NaCl. Therefore, hsp 90 seems to be responsible for the surface charge characteristics of the nontransformed GR.
大鼠肝脏中转化的糖皮质激素受体（GR）在硫酸铵饱和度为30%时沉淀，在甘油梯度离心中沉降系数为4.3 S，而非转化的GR在较高硫酸铵浓度（40 - 50%饱和度）下沉淀，在梯度离心中沉降系数为8.6 S。十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示，热休克蛋白90（hsp 90）在硫酸铵饱和度为40 - 50%时沉淀。此外，hsp 90和非转化的GR在相似盐浓度（0.22 - 0.23 M NaCl）下从DEAE高效离子交换色谱中洗脱，而转化的GR在0.1 M NaCl下洗脱。因此，hsp 90似乎决定了非转化GR的表面电荷特性。
