Amino Acids and Peptides. XII. Synthesis of C-Terminal Decapeptide of Bovine Pancreatic Ribonuclease A (RNase A) and Its Analogs and Determination of Their Ability to Reactivate Des (121-124) RNase A

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概要

• 論文の詳細を見る

• A decapeptide corresponding to the C-terminal sequence (residues 115-124) of bovine pancreatic ribonuclease A (RNase A) and four analogs in which Asp-121 is replaced by Asn, Glu, Gln and Ala were synthesized by the fragment condensation procedure, and their abilities to reactivate RNase A from which the last 4 residues, Asp-Ala-Ser-Val, had been removed were examined. Asp-decapeptide (I) and Glu-decapeptide (III) bound with inactivated RNase 1-120 non-covalently and exhibited hydrolytic activity towards cyclic 2', 3'-cytidylic acid. In contrast, Asn-decapeptide (II), Gln-decapeptide (IV) and Ala-decapeptide (V) did not show any ability to restore the activity of RNase A 1-120. Our systematic syntheses of the C-terminal decapeptide of RNase A and its analogs indicate a very important role of the free carboxyl group at position 121 of RNase A for manifestation of RNase activity.

• 社団法人日本薬学会の論文
• 1984-11-25

著者

• 岡田 芳男

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 入江 昌親

  Department of Microbiology, Hoshi College of Pharmacy

• 手納 直規

  Faculty of Pharmaceutical Sciences

• 森 裕美子

  Department Of Microbiology Hoshi College Of Pharmacy

• 宮尾 純子

  Department of Microbiology, Hoshi College of Pharmacy

• 入江 昌親

  Department Of Chemistry Institute For Infectious Diseases University Of Tokyo

• 手納 直規

  Faculty Of Pharmaceutical Sciences Kobe-gakuin University

• 宮尾 純子

  Department Of Microbiology Hoshi College Of Pharmacy

• 入江 昌親

  Department Of Microbiology Hoshi College Of Pharmacy

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