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Semisynthetic studies on bovine pancreatic ribonuclease
| Content Provider | Scilit |
|---|---|
| Author | Bello, Carlo Lucchiari, Adriana Buso, Orfeo Tonellato, Mauro |
| Copyright Year | 2009 |
| Description | Journal: International journal of peptide and protein research 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. |
| Ending Page | 71 |
| Starting Page | 61 |
| ISSN | 2573508X |
| DOI | 10.1111/j.1399-3011.1984.tb02693.x |
| Journal | International journal of peptide and protein research |
| Issue Number | 1 |
| Volume Number | 23 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2009-01-12 |
| Access Restriction | Open |
| Subject Keyword | Journal: International journal of peptide and protein research Medicinal Chemistry Arginine‐peptide Coupling Bovine Pancreatic Ribonuclease Protein Semisynthesis Solid‐phase Fragment Condensation |
| Content Type | Text |
| Resource Type | Article |
