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J. Biochem, 1980, Vol. 87, No. 4 1079-1087
© 1980 Japanese Biochemical Society

research-article

Chemical Modification of Tryptophan Residues in Ribonuclease from a Rhizopus sp.1

Akihiro SANDA and Masachika IRIE

Department of Microbiology, Hoshi College of Pharmacy Ebara, Shinagawa-ku, Tokyo 142

Tryptophan residues in ribonuclease from a Rhizopus sp. (RNase Rh) were modified by NBS, H2O2-dioxane, o-nitrophenylsulfenyl chloride (NPS-Cl) and the relation between the extent of modification and enzymatic activity was studied in each case.

By extrapolation of the modified tryptophan residue-enzymatic activity curve to a completely inactive state, it was found that modification of 1–2 tryptophan residues is responsible for loss of enzymatic activity.

RNase Rh was partly protected from modification by H2O2-dioxane (pH 8.4) and NPS-Cl (pH 3.5) when in the presence of 2'-AMP and the fluorescence emission spectrum of RNase Rh was quenched by adding 2'-AMP. It seems, therefore, that 1 or 2 tryptophan residues are involved in the active site of RNase Rh or are located near the active site.

The solvent perturbation difference spectra of RNase Rh were measured using ethylene glycol and D2O as perturbants. The results indicated that 1.2 tryptophan residues for D2O and 1.9 tryptophan residues for ethylene glycol were exposed to the solvents. These data show that about 1.2–1.9 tryptophan residues are exposed to the solvent and their modification causes loss in enzymatic activity.

1This study was supported in part by a grant from Yamada Science Foundation.


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