Studies on the Active Site of Papain. V. Photooxidation of Histidine Residues

概要

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1) The present research has been planed to demonstrate the importance of histidine residues on enzyme activity of papain by means of photooxidation. 2) Papain was rapidly inactivated by methylene blue-sensitized photooxidation. 3) The rate of photo-sensitized inactivation was pH dependent, and about one histidine residue per molecule of papain was lost when complete inactivation took place. 4) Mercuripapain was not inactivated by methylene blue-sensitized photooxidation, and the histidine residue was not affected in the illuminated mercuripapain. 5) These results indicate that the modification of a histidine residue by photooxidation cause loss of the enzyme activity for hydrolysis of benzoyl-L-arginine amide. 6) The state of the histidine residue in the active site of papain is discussed to explain the results of the photooxidation studies described here.
公益社団法人日本薬学会の論文
1975-05-25