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J. Biochem, 1970, Vol. 68, No. 1 63-67
© 1970 Japanese Biochemical Society

research-article

Photooxidation of Ribonuclease T1 in the Presence of Substrate Analog

Keizo WAKU and Yasuo NAKAZAWA

The School of Medicine, Tokyo Medical and Dental University, Bunkyo-ku, Tokyo

Ribonuclease T1 [EC 2. 7. 7. 26] was photooxidized with and without protection by the substrate analog, a mixture of guanosine 2‘-phosphate and guanosine 3’-phosphate. In the absence of the substrate analog, the enzymatic activity gradually decreased with loss of two to three histidine residues, while in the presence of the substrate analog, full activity was maintained and two histidine residues were protected against photo-oxidation. The tryptophan residue was oxidized with simultaneous Oj-uptake and the rate was scarcely affected by the presence of the substrate analog. These results demonstrate that two histidine residues are involved in the active centre of ribonuclease T1 but that is not involved.


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