Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations
D Piszkiewicz, M Landon, EL Smith - Biochemical and biophysical research …, 1970 - Elsevier
Abstract Aspartyl-proline peptide bonds have been found to be hydrolyzed during exposure
to low pH values under conditions where other aspartyl bonds are stable. The mechanism of
this hydrolytic reaction is concluded to proceed via intramolecular catalysis by carboxylate
to low pH values under conditions where other aspartyl bonds are stable. The mechanism of
this hydrolytic reaction is concluded to proceed via intramolecular catalysis by carboxylate
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