Specific chemical cleavage of asparaginyl and glycyl-glycine bonds in peptides and proteins by anhydrous hydrazine vapor.
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.
Miyatake
N
N
Research Institute for Biosciences, Science University of Tokyo, Chiba.
Satake
K
K
Kamo
M
M
Tsugita
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000812:Anhydrides; D000818:Animals; D001216:Asparagine / Q000737:chemistry*; D005591:Chemical Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D005998:Glycine / Q000737:chemistry*; D006834:Hydrazines / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D000596:Amino Acids; D000812:Anhydrides; D006834:Hydrazines; D010455:Peptides; D011506:Proteins; C029424:hydrazine; D001216:Asparagine; D005998:Glycine