Several enzymatically active water-insoluble ribonuclease T1 (ribonucleate guaninenucleotide-2′-transferase (cyclizing), EC 184.108.40.206) derivatives were prepared. One of these, Sepharose T1, which was prepared by chemically coupling ribonuclease T1 to Sepharose, was further characterized. The enzyme derivative was stable and had no detectable residual soluble enzymatic activity. Substrate specificity of the enzyme derivative remained unaltered. Kinetic values were similar to the free, native enzyme.
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