PMID: 8462549Mar 15, 1993Paper

Removal of N-terminal formyl groups and deblocking of pyrrolidone carboxylic acid of proteins with anhydrous hydrazine vapor

European Journal of Biochemistry
N MiyatakeA Tsugita

Abstract

Many proteins have a blocked alpha-amino group which renders them inaccessible to sequence analysis by the classical Edman degradation procedure. Blockage typically occurs when the alpha-amino groups are acylated with acetyl or formyl groups or when the N-terminal residue is pyrrolidone carboxylic acid formed by cyclization of glutamine. We have found that N-formyl groups of proteins and peptides can be removed by exposure to hydrazine vapor at -5 degrees C for 8 h. Under these conditions, peptide-bond cleavage or modification of the constituent amino-acid residues does not occur. Deblocking of N-terminal pyrrolidone carboxylate residues by conversion to gamma-hydrazidyl glutamic acid can be achieved by exposure to hydrazine vapor at 20 degrees C for 4 h. These conditions cause partial modification of asparagine and glutamine residues to their corresponding hydrazides, and conversion of arginine residues to ornithine.

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Citations

May 1, 1994·Electrophoresis·A TsugitaY Nozu
Oct 1, 1995·Journal of Biomedical Science·N. FukayaK. Tabuchi
Apr 23, 2003·Acta Biologica Hungarica·A MádiL Fésüs
Mar 15, 1995·European Journal of Biochemistry·A E ProudfootT N Wells
Jan 19, 2008·Proteomics·Thierry Meinnel, Carmela Giglione
Jun 11, 2005·Biotechnology and Bioengineering·Anne IncampsEric Quéméneur
Apr 23, 2008·Current Protocols in Protein Science·E FowlerF Wold
Mar 15, 2011·Current Protocols in Protein Science·Joseph W LeoneChristopher C Q Chin
Jan 27, 1999·Biochimica Et Biophysica Acta·P M Cummins, B O'Connor

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