抄録
During the course of cytochemical studies on ornithine carbamoyl-transferase (OCT) activity in the briefly fixed rat liver with glutaraldehyde perfusion, carbamoyl phosphate, one of the substrate of OCT, was found to be hydrolyzed enzymatically in the endoplasmic reticulum and the nuclear envelope of hepatocytes independently of OCT activity. The nature of the activity was analyzed: (1) The activity was abolished by pretreatment of the sections at pH 5.0 and 37°C. (2) Heat treatment at 50°C inactivated the activity. (3) Cold acetone and sodium fluoride also destroyed the activity. (4) The pH optimum was between pH 6.0 and 7.0. These results were compared to the characteristics of glucose 6-phosphatase and acyl-phosphatase.
