CYTOCHEMICAL STUDIES ON HYDROLYSIS OF CARBAMOYL PHOSPHATE IN RAT LIVER
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概要
- 論文の詳細を見る
During the course of cytochemical studies on ornithine carbamoyltransferase (OCT) activity in the briefly fixed rat liver with glutaraldehydeperfusion, 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℃. (2) Heat treatment at 50℃ 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 acylphosphatase.
- 日本組織細胞化学会の論文
著者
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Mizutani Akira
Department Of Morphology Institute For Developmental Research Aichi Prefectural Colony
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Fujita Hajime
Department Of Cytochemistry Chest Disease Research Institute Kyoto University Kyoto
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Mizutani Akira
Department Of Cytochemistry Chest Disease Research Institute Kyoto University
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Mizutani Akira
Department Of Cytochemistry Chest Disease Research Institute Kyoto University Kyoto
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