Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease

Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease

1962

REP.G1296

1. Cyanogen bromide selectively cleaves peptide bonds next to methionine. The reaction proceeds at room temperature in aqueous solution in the acidic pH range. No side reactions have been observed. The new method has been applied to bovine pancreatic ribonuclease. 2. All four methionine peptide bonds present in ribonuclease are cleaved with cyanogen bromide. The fragments resulting from this cleavage may be separated by gel filtration on Sephadex Cyclodextran. 3. Amino acid analyses and end group determination of the isolated and purified fragments have led to results which disagree with the previously published sequence for ribonuclease. 4. The data lead to a revised sequence of ribonuclease for positions 11 through 14: -Glu-NH2(?)-His-Met-Asp-.

v.237(6):1856-1860, JOURNAL OF BIOLOGICAL CHEMISTRY

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