A-11. Prostaglandin合成酵素-特にその活性化因子について-

抄録

The formation of prostaglandin E₁ from bishomo-γ-linolenic acid by the microsomal fraction of bovine vesicular gland, required the simultaneous presence of glutathione, hydroquinone and hemoglobin as reported by other investigators. A new activator which could replace hydroquinone, was isolated and purified approximately 100 fold from the soluble fraction of bovine vesicular gland. This activator was retained upon Sephadex G-200 column chromatography, but eluted faster than hemoglobin. Its activity was lost by heating for 5 min over 60°. Pronase treatment did not affect the activity or the molecular weight of the activator. The inhibition of prostaglandin E₁ synthesis by indomethacin, aspirin and sodium salicylate was observed at lower concentrations in the presence of the activator than in its absence. The activator was adsorbed to Sepharose 4B coupled with indomethacin, and was eluted by increasing the salt concentration.