TURNIP PEROXIDASE:III. THE PHYSICOCHEMICAL PROPERTIES OF CRYSTALLINE TURNIP PEROXIDASE D

J-STAGE
  • HOSOYA TOICHIRO
    Department of Physical Chemistry, Institute of Endocrinology, Gunma University

この論文をさがす

説明

1. The absorption spectra of crystalline turnip peroxidase D were measured for its alkaline form and for its compounds with carbon monoxide, cyanide, azide and fluoride. They were found to agree very closely with those of horseradish peroxidase. The pK value of the dissociation of a hydrogen ion from the water molecule linked to the iron atom of hematin was found to be 10.28 at an ionic strength of 0.1.<br> 2. The diffusion constant (D20, W) of the enzyme was found to be 8.37×10-7cm2. sec-1.<br> 3. The sedimentation constant (S20, W) of the enzyme was found to be 3.58 S or 3.55 S, assuming the partial specific volume to be 0.75 or 0.70, respectively.<br> 4. Using the above values, the molecular weight was calculated to be 41, 500 or 34, 300 and the frictional ratio 1.10 or 1.23, respectively.<br> The author wishes to express his sincere thanks to Prof. N. Ui for his invaluable advice and encouragement. This study was aided in part by a Grant-in-Aid for Scientific Research from the Ministry of Education given to the Research Group on "Mechanism of Enzyme Action".

収録刊行物

詳細情報 詳細情報について

問題の指摘

ページトップへ