title: C-terminal amidation of calcitonin by carboxypeptidase Y catalyzed transpeptidation with a photocleavable nucleophile.
abstract: The C-terminal amidation of calcitonin represents an important technological problem. A method using a serine carboxypeptidase-catalyzed transpeptidation reaction in combination with photochemical cleavage to give the warranted peptide amide is described. The overall yield is higher than 95%.
authors: University of Copenhagen, Denmark.
authors: D B
authors: DB
authors: Henriksen
authors: M
authors: M
authors: Rolland
authors: M H
authors: MH
authors: Jakobsen
authors: O
authors: O
authors: Buchardt
authors: K
authors: K
authors: Breddam
mesh_terms: D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D002116:Calcitonin / Q000737:chemistry*; D002268:Carboxypeptidases / Q000737:chemistry*; D005998:Glycine / Q000031:analogs & derivatives* / Q000737:chemistry; D006834:Hydrazines / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009578:Nitrobenzenes / Q000737:chemistry*; D010777:Photochemistry
chemical_list: D000577:Amides; D006834:Hydrazines; D009578:Nitrobenzenes; C079588:2-nitrophenylglycinamide; C029424:hydrazine; D002116:Calcitonin; D002268:Carboxypeptidases; C022633:serine carboxypeptidase; D005998:Glycine