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6660836 
Journal Article 
AN APPROACH TO THE SPECIFIC CLEAVAGE OF PEPTIDE BONDS. II. SPECIFIC CLEAVAGE OF PEPTIDE CHAINS BASED ON THE HYDROGEN FLUORIDE-INDUCED NITROGEN TO OXYGEN ACYL SHIFT 
Lenard, J; Hess, GP; , 
1964 
Yes 
Journal of Biological Chemistry
ISSN: 0021-9258
EISSN: 1083-351X 
239 
(10) 
3275-3281 
English 
14245373 
BCI:BCI19654600014484 
A method for the specific cleavage of peptide bonds at serine residues is demonstrated with oxidized A and B chains of insulin and with [alpha] melanocyte-stimulating hormone. In the procedure, methanolic anhydrous hydrogen fluoride is used to induce the N to O shift, and after blockage of the free amino groups by formylation, aqueous piperidine is used . to effect cleavage. Prior oxidation of methionyl residues prevents cleavage of methionyl peptide bonds, which otherwise occurs in high yields in hydrogen fluoride (Lenard, John, and George P. Hess, Biochem. and Biophys. Research Communs., 14, 498(1964)). Yields of 80 to 91% of the theoretically-expected O-acyi products were obtained. All amino acid residues present in the peptides were shown to be stable, except for the tryptophyl reside, which was partially destroyed under the experimental conditions used. || ABSTRACT AUTHORS: Authors