Abstract:
:In order to obtain information on the nature of the amino acid residues involved in the activity of ribonuclease U1 [EC 3.1.4.8], various chemical modifications of the enzyme were carried out. RNase U1 was inactivated by reaction with iodoacetate at pH 5.5 with concomitant incorporation of 1 carboxymethyl group per molecule of the enzyme. The residue specifically modified by iodoacetate was identified as one of the glutamic acid residues, as in the case of RNase T1. The enzyme was also inactivated extensively by reaction with iodoacetamide at pH 8.0 with the loss of about one residue each of histidine and lysine. When RNase U1 was treated with a large excess of phenylglyoxal, the enzymatic activity and binding ability toward 3'-GMP were lost, with simultaneous modification of about 1 residue of arginine. The reaction of citraconic anhydride with RNase U1 led to the loss of enzymatic activity and modification of about 1 residue of lysine. The inactivated enzyme, however, retained binding ability toward 3'-GMP. These results indicate that there are marked similarities in the active sites of RNases T1 and U1.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Hashimoto J,Takahashi Kdoi
10.1093/oxfordjournals.jbchem.a131544subject
Has Abstractpub_date
1977-04-01 00:00:00pages
1175-80issue
4eissn
0021-924Xissn
1756-2651journal_volume
81pub_type
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更新日期:1998-08-01 00:00:00
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更新日期:1993-10-01 00:00:00
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更新日期:1981-02-01 00:00:00
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更新日期:2009-12-01 00:00:00