抄録
The oxidase activity of crystalline porcine caeruloplasmin was studied spectroscopically with p-phenylenediamine as the substrate. Borate ion inhibited the oxidase activity and the inhibition was found to be of reversible nature. The functional relationship obtained between borate concentration and the degree of inhibition indicated that the inhibition is the non-competitive type and occurs by combination of a borate ion with a sugar contained in the caeruloplasmin molecule. The structure of the active center near the copper atom of the molecule is discussed, refering the previous results described in this series of reports.
The author wishes to express his deep gratitude to Prof. S. Hattori, University of Tokyo, and Prof. T. Sato, Prof. K. Shibata and Dr. Nagahisa, Tokyo Institute of Technology, for their valuable advice and interest throughout this investigation. He is also thankful to Dr. Kanazawa, Mr. Kaya and Mr. Kikuclii for their help in carrying out this study.
