1987Chemical and Pharmaceutical BulletinOpen access

Amino acids and peptides. XIV Synthesis and biological activity of three S-peptide analogues of bovine pancreatic ribonuclease A (RNase A).

Naoki Teno, Satoshi Tsuboi, Tomoko Shimamura, Yoshio Okada, YOSHIMI YANAGIDA, Makiko YOSHINAGA, Kazuko Ohgi, Masachika IRIE

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Abstract

Three S-peptide analogues of bovine pancreatic ribonuclease A (RNase A), [Nle1] [Lys7] S-peptide (I), [Lys1] [Nle7] S-peptide (II) and [Nle1] [Nle7] S-peptide (III), were synthesized by the fragment condensation method and their ability to reactivate S-protein was examined. It was found that Lys1 and Lys7 both have roles in the reactivation of S-protein.

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Three S-peptide analogues of bovine pancreatic ribonuclease A (RNase A), [Nle1] [Lys7] S-peptide (I), [Lys1] [Nle7] S-peptide (II) and [Nle1] [Nle7] S-peptide (III), were synthesized by the fragment condensation method and their ability to reactivate S-protein was examined. It was found that Lys1 and Lys7 both have roles in the reactivation of S-protein.

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Available abstract

Three S-peptide analogues of bovine pancreatic ribonuclease A (RNase A), [Nle1] [Lys7] S-peptide (I), [Lys1] [Nle7] S-peptide (II) and [Nle1] [Nle7] S-peptide (III), were synthesized by the fragment condensation method and their ability to reactivate S-protein was examined. It was found that Lys1 and Lys7 both have roles in the reactivation of S-protein.

Key concepts: Bovine pancreatic ribonuclease, S-tag, Chemistry, RNase P, Peptide, Ribonuclease, Pancreatic ribonuclease, Ribonuclease III

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