Semisynthetic studies on bovine pancreatic ribonuclease.
The S-peptide of the enzyme bovine pancreatic ribonuclease has been used as a model for covalent semisynthesis. Methods for side-chain protection, enzymatic cleavage of the peptide chain at the level of the single arginine-10 and for selective deprotection of the alpha-carboxyl function of this residue, have been examined. The partially protected [1-10] sequence has been coupled to a solid-phase generated [11-15] sequence attached to the polymer. After deblocking from the solid-support, the [1-15] semisynthetic peptide was complexed with native S-protein to give a complex with high biological activity.
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine; D002417:Cattle; D007202:Indicators and Reagents; D010446:Peptide Fragments / Q000138:chemical synthesis*; D012259:Ribonuclease, Pancreatic / Q000138:chemical synthesis* / Q000378:metabolism; D014357:Trypsin
D007202:Indicators and Reagents; D010446:Peptide Fragments; D001120:Arginine; D012259:Ribonuclease, Pancreatic; D014357:Trypsin