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Reactivation of des(119–124) Ribonuclease A by Mixture with Synthetic COOH-terminal Peptides; the Role of Phenylalanine-120

From the ¹ From The Rockefeller University, New York, New York 10021

Several peptides contained within the amino acid sequence -Glu-Gly-Asn-Pro-Tyr-Val-Pro-Val-His-Phe-Asp-Ala-Ser-Val-OH at the carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan: [Leu¹²⁰]-RNase 111–124, [Ile¹²⁰]-RNase 111–124, [Trp¹²⁰]-RNase 111–124, [Ile¹²⁰]-RNase 113–124, [Leu¹²⁰]-RNase 115–124, [Ile¹²⁰]-RNase 115–124, [Trp¹²⁰]-RNase 115–124. The peptides were examined for their ability to regenerate enzymatic activity when mixed with RNase 1–118 which had been prepared by enzymatic degradation of RNase A. A study of the dissociation constants of the peptide-protein complexes, of the Michaelis constants of the complexes with cyclic 2', 3'-cytidylic acid, and of the inhibition constants with 2'-cytidylic acid led to the conclusion that Phe¹²⁰ plays an important role in binding the peptide and protein and in aligning the catalytic site of the complex, but that it does not have a specific effect on binding of substrate.

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