STUDIES ON HISTIDINE RESIDUES IN HEMEPROTEINS RELATED TO THEIR ACTIVITIES

  • NAKATANI MISAKO
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyushu University|Research Institute of Angiocardiology, Faculty of Medicine, Kyushu University

Description

1. Catalase was treated with bromoacetic acid in the presence of MgO at pH 9. At these conditions, 35 per cent of total diazocoupling groups reacted, and about 20 per cent decrease of the total enzyme activity was resulted.<br> 2. The absorption spectrum changed slightly after the carboxymethylation of the native catalase, whereas 2M urea-denatured catalase showed a remarkable decrease after the carboxymethylation.<br> 3. After treatments of catalase with 2, 6 and 8M urea respectively, additional 11 to 20 per cent of the histidines (10 to 19 moles in one mole of catalase) reacted with bromoacetic acid in comparison with untreated sample. It seems that these urea activated histidine residues are masked in native state, a part of which might be related with secondary structure of the protein.<br> The author wishes to express her gratitude to Prof. Y. Oshima and Prof. M. Funatsu for their invaluable advice and criticism during the course of this work, and to Mr. S. Abe for his assistance in the preparation of catalase.

Journal

Details 詳細情報について

  • CRID
    1570291228033828480
  • NII Article ID
    130006876721
  • Text Lang
    en
  • Data Source
    • CiNii Articles

Report a problem

Back to top