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Cleavage of a model peptide at its glycine residue by alkaline mercuric oxycyanide.
Int J Pept Protein Res
July 1989
Department of Biochemistry, Albany Medical College, New York.
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.
View Article and Find Full Text PDFA series of metallated arenes bearing sigma-bonded tin, mercury, germanium, boron, or silicon were evaluated as labeling substrates for the generator-produced positron emitter 122I(t1/2 = 3.6 min). Using dichloramine-T with 122I, radiochemical yields exceeding 90% were achieved after 1 min at 25 degrees C using stannylated or mercurated arenes in ethanol, or germylated arenes in acidic solvent.
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