Isolation and identification of the cyanogen bromide peptides of D-glyceraldehyde-3-phosphate dehydrogenase from human muscle.
D-Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) from human muscle was S-carboxymethylated, cleaved with cyanogen bromide and citraconylated. The enzymatic protein contains 344 amino acid residues, nine of which are methionines. The respective ten cyanogen bromide fragments have been isolated and characterized. Each peptide was purified to homogeneity by Bio-Gel chromatography, high voltage electrophoresis and descending paper chromatography, and characterized by electrochromatography, N-terminal sequence and amino acid composition.
D002850:Chromatography, Gel / Q000379:methods; D002854:Chromatography, Paper; D003488:Cyanogen Bromide / Q000302:isolation & purification*; D004586:Electrophoresis / Q000379:methods; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis*; D006801:Humans; D009132:Muscles / Q000201:enzymology*; D010455:Peptides / Q000302:isolation & purification*
D010455:Peptides; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D003488:Cyanogen Bromide