Isolation and characterization of the 'photosynthetic' phosphoglycerate kinase from Beta vulgaris.
1. Phosphoglycerate kinase has been isolated from a photosynthetic plant tissue, Beta vulgaris leaves. The purification procedure is described. 2. The best preparation had no detectable impurity on electrophoresis, and had a specific activity comparable with the same enzyme from other sources. 3. The molecular weight was not distinguishably different from that of the yeast or muscle enzyme, as measured by polyacrylamide-dodecylsulphate electrophoresis. Measurement of aromatic and sulphydryl residues indicated a close similarity with the yeast enzyme. The enzyme appears to have substantially lower isoelectric point than phosphoglycerate kinases from other sources. 4. Kinetic studies indicated that the affinities for the substrates MgATP2- and 3-phosphoglycerate were not significantly different from those of the 'glycolytic' yeast enzyme. There was no evidence that the B. vulgaris enzyme had specific properties making it more suitable for its gluconeogenic rather than glycolytic role.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D002413:Cations, Divalent; D002846:Chromatography, Affinity; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D010735:Phosphoglycerate Kinase / Q000302:isolation & purification / Q000378:metabolism*; D010788:Photosynthesis; D010944:Plants / Q000201:enzymology*; D013045:Species Specificity
D002413:Cations, Divalent; D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase; D008274:Magnesium