title: Structural studies on yeast 3-phosphoglycerate kinase. Isolation by affinity chromatography and characterization of the peptides produced by cyanogen bromide cleavage. Location of the single cysteinyl residue in the primary structure.
abstract: Cyanogen bromide cleavage of yeast 3-phosphoglycerate kinase yielded four fragments which account for the amino acid composition of the entire molecule. These results are consistent with a single polypeptide chain of molecular weight 42 000. Affinity chromatography on Sepharose-mercurial followed by gel filtration on Sephadex was used with success for separation of peptides. The carboxyl and N-terminal fragments were characterized. The N-terminal fragment contained the single cysteinyl residue of the protein. After cyanylation and subsequent cleavage, this cysteinyl residue was located near position 100.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002846:Chromatography, Affinity; D003488:Cyanogen Bromide; D003545:Cysteine / Q000032:analysis*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010735:Phosphoglycerate Kinase / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D010735:Phosphoglycerate Kinase; D003545:Cysteine; D003488:Cyanogen Bromide