Evidence for the Presence of a Histidine Residue having pK_a 7 in the Active Site of a Ribonuclease from a Rhizopus sp.
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概要
- 論文の詳細を見る
The kinetic parameters, K_m and log V_<max>, of the cleavage of dinucleoside phosphates, GpU, GpC and ApU, by RNase Rh from a Rhizopus sp. were measured at various pH's. Analysis of the pH profiles of K_m and V_<max> of these dinucleoside phosphates according to Dixon's theory suggested that two functional groups having pK_a values of 7.0-7.3 and 3.25-3.5 are present in the active site of RNase Rh. The former value may correspond to a histidine residue. The pH dependence of the rates of inactivation of RNase Rh by photoxidation and carbethoxylation also indicated that a functional group having pK_a about 7.0 was involved in the active site. Amino acid analysis of photooxidized RNase Rh showed that only a histidine residue had been destroyed. In the carbethoxylation of RNase Rh, the formation of carbethoxyhistidine caused a corresponding loss of activity of RNase Rh without modification of tyrosyl residues. It was concluded that a histidine residue having pK_a about 7.0 is involved in the active site of RNase Rh.
- 公益社団法人日本薬学会の論文
- 1979-10-25
著者
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入江 昌親
Department of Microbiology, Hoshi College of Pharmacy
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入江 昌親
星薬科大
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入江 昌親
Department Of Chemistry Institute For Infectious Diseases University Of Tokyo
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三田 明弘
麻布大学・生化学研究室
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三田 明弘
Department of Microbiology, Hoshi College of Pharmacy
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