Specific chemical cleavage of asparaginyl and glycyl-glycine bonds in peptides and proteins by anhydrous hydrazine vapor

J Biochem. 1994 Feb;115(2):208-12. doi: 10.1093/oxfordjournals.jbchem.a124319.

Abstract

Hydrazinolysis of peptide or protein has been used for C-terminal amino acid determination by Akabori et al. (1952). In this study, proteins were reacted with anhydrous hydrazine vapor at 20 degrees C for 16 h. Asparaginyl linkages were cleaved. Asparagine and glutamine were converted to their hydrazides, beta-hydrazidyl aspartic acid and gamma-hydrazidyl glutamic acid, respectively, even under milder conditions. The former hydrazide cyclizes to a 6-membered ring, asparaginyl bond at the carboxyl side. Other cleavages, including the glycyl-glycine bond, were also observed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Anhydrides
  • Animals
  • Asparagine / chemistry*
  • Chemical Fractionation
  • Electrophoresis, Polyacrylamide Gel
  • Glycine / chemistry*
  • Hydrazines / chemistry*
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Proteins / chemistry*
  • Spectrometry, Mass, Fast Atom Bombardment

Substances

  • Amino Acids
  • Anhydrides
  • Hydrazines
  • Peptides
  • Proteins
  • hydrazine
  • Asparagine
  • Glycine