Syntheses of polypeptides corresponding to ribonuclease T1 and its analog, [59-tyrosine]-ribonuclease T1

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Abstract

Two polypeptides with the sequence of ribonuclease T1 and its analog, [59-tyrosine]-ribonuclease T1 were prepared by the solid-phase method. After purification by gel filtration and ion exchange chromatography, the synthetic peptides afforded similar patterns on paper and disc electrophoreses to those of natural enzyme. Further purification of the peptide corresponding to ribonuclease T1 raised the specific activity to 59% for RNA and 44% for guanosine 2′,3′-cyclic phosphate. In case of [59-tyrosine]-ribonuclease T1, the activity was raised to 61% and 57%, respectively.

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