Isotope exchange at equilibrium studies with rat kidney gamma-glutamylcysteine synthetase.
The kinetic binding mechanism of rat kidney gamma-glutamylcysteine synthetase has been evaluated by isotope exchange at equilibrium studies. The results are consistent with a Random BC mechanism as suggested previously (Yip, B. P., and Rudolph, F. B. (1976) J. Biol. Chem. 251, 3563-3568). The purification procedure for the enzyme was modified to remove contaminating adenylate kinase prior to isotope exchange studies.
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000818:Animals; D002250:Carbon Radioisotopes; D005721:Glutamate-Cysteine Ligase / Q000302:isolation & purification / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D010453:Peptide Synthases / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D011865:Radioisotope Dilution Technique; D051381:Rats
D002250:Carbon Radioisotopes; D010761:Phosphorus Radioisotopes; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D010453:Peptide Synthases; D005721:Glutamate-Cysteine Ligase