Glyceraldehyde-3-phosphate dehydrogenase from human muscle: cleavage of tryptophanyl peptides with o-iodosobenzoic acid.
The new procedure of protein fragmentation with o-iodosobenzoic acid (Mahoney & Hermodson, 1979; Biochemistry, 18, 3810-3814) was used to split three tryptophanyl peptide bonds in glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) from human skeletal muscle. The mixture obtained was separated into four homogeneous peptides by a one-step chromatographic procedure. High specificity of the cleavage reaction was proved by the amino acid analysis and determination of the N-terminal sequence of the peptide products. Both specificity ahd high yield obtained by this procedure confirmed its utility in the establishment of the protein primary structure.
D000596:Amino Acids / Q000032:analysis; D004586:Electrophoresis / Q000379:methods; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis*; D006801:Humans; D006868:Hydrolysis; D007463:Iodobenzoates; D009132:Muscles / Q000201:enzymology*; D010455:Peptides / Q000302:isolation & purification*; D014364:Tryptophan
D000596:Amino Acids; D007463:Iodobenzoates; D010455:Peptides; C008154:2-iodosobenzoic acid; D014364:Tryptophan; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases