title: Cleavage of a model peptide at its glycine residue by alkaline mercuric oxycyanide.
abstract: Treatment of peptides with excess HgO in the presence of alkaline cyanide leads to cleavage of the peptides at glycine residues. The reaction appears to involve both C- and N-mercuration with subsequent release of 2 mol mercury per mol of glycine. An intermediate glyoxylic acid residue in Schiff base linkage is postulated. Treatment of the heptapeptide Phe-Ala-Lys-Gly-Leu-Asp-Val with alkaline HgO and KCN for 6 h at 25 degrees resulted in greater than 90% cleavage, and the resultant reaction products were separated by reverse phase chromatography and identified by amino acid analysis. N-terminal products were approximately equimolar Phe-Ala-Lys, Phe-Ala-Lys-Gly, and Phe-Ala-Lys-amide. C-terminal products were predominantly Leu-Asp-Val (63%), plus Gly-Leu-Asp-Val (9%), and oxalyl-Leu-Asp-Val (8%). This method may be useful for cleavage of peptides or proteins containing glycine residues.
authors: Department of Biochemistry, Albany Medical College, New York.
authors: S R
authors: SR
authors: Krystek
authors: T T
authors: TT
authors: Andersen
authors: P B
authors: PB
authors: Weber
mesh_terms: D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D003486:Cyanides; D005998:Glycine; D006863:Hydrogen-Ion Concentration; D008628:Mercury; D017669:Mercury Compounds; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides; D010087:Oxides; D010446:Peptide Fragments / Q000302:isolation & purification; D011190:Potassium Cyanide
chemical_list: D003486:Cyanides; D017669:Mercury Compounds; D009842:Oligopeptides; D010087:Oxides; D010446:Peptide Fragments; D008628:Mercury; C019468:mercuric oxide; D011190:Potassium Cyanide; D005998:Glycine