Studies on the Specificity of Ribonuclease from Rhizopus sp.

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概要

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• In order to investigate the base specificity of the RNase from Rhizopus sp. (RNase Rh), its kinetic parameters were measured with 16 dinucleoside phosphates (XpY, where X or Y represents one of adenosine, guanosine, uridine and cytidine) as substrates at pH 5.5 and 25°. The average K_m values of ApY, GpY, CpY and UpY increased in the order A, G, C and U. The average K_m values of ApY, GpY, CpY and UpY increased in the order A, G, U and C. The average V_<max> values of ApY, GpY, CpY and UpY were larger for dinucleoside phosphates having A and G at X. However, the average V_<max> values of XpA, XpG, XpC and XpU were relatively constant. It was concluded that the X base in XpY contributes mainly to the specificity of the enzyme and the Y base may modify this somewhat. The K_1 values of various nucleotides towards RNase Rh were measured at pH 5.5. These compounds inhibited RNase Rh competitively. Although the inhibitory effect depends on the base, sugar and location of the phosphate moiety, for a given location of phosphate on the sugar, the K_1 values of ribonucleotides decreased in the order U, C, G and A and those of deoxyribonucleotides decreased in the order T, C, G and A. These data also show that purine bases, especially adenine, have high affinities for RNase Rh.

• 公益社団法人日本薬学会の論文
• 1979-09-25

著者

• 入江 昌親

  Department of Microbiology, Hoshi College of Pharmacy

• 入江 昌親

  星薬科大

• 入江 昌親

  Department Of Chemistry Institute For Infectious Diseases University Of Tokyo

• 武田 麗子

  Department Of Microbiology Hoshi College Of Pharmacy

• 三田 明弘

  麻布大学・生化学研究室

• 三田 明弘

  Department of Microbiology, Hoshi College of Pharmacy

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• グルコアミラ-ゼの多様化について
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