Abstract
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.
