A new assay to measure RNA N-glycosidase activity.
We have developed a convenient procedure to measure the activity of Ricin A-chain and other enzymes with RNA N-glycosidase activity. The method is based on the use of a tritiated oligoribonucleotide as a substrate. The enzymatic activity is directly determined by measuring the release of adenine from the substrate. This method should prove useful in the study of the molecular mechanism of action of Ricin A and other RNA N-glycosidases.
Endo
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Department of Biochemistry, Yamanashi Medical College, Japan.
Glück
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D000818:Animals; D001483:Base Sequence; D002855:Chromatography, Thin Layer; D008722:Methods; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009843:Oligoribonucleotides / Q000378:metabolism; D012339:RNA, Ribosomal, 28S / Q000378:metabolism; D051381:Rats; D054788:Ribosome Inactivating Proteins; D012276:Ricin / Q000378:metabolism
D009843:Oligoribonucleotides; D012339:RNA, Ribosomal, 28S; D012276:Ricin; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins