Abstract
Fraction I protein from leaves of Spinacia oleracea was purified to electrophoretic homogeneity using ammonium sulphate fractionation, ion-exchange chromatography, and gel filtration. The purified protein exhibited a 280 nm/260 nm ratio of 1-81 and a sedimentation coefficient of 20-6S. The stoichiometry of the ribulose-l,5-bisphosphate oxygenase reaction was determined for 02 consumption and phosphoglycolic and phosphoglyceric acid production. For every 0-87 ± 0-07 /?mol 02 consumed there were 0-83 ± 0-04 /?mol phosphoglycolic acid and 0-87 ± 0-13 /?mol phosphoglyceric acid produced. Hydroxylapatite column chromatography was found to be effective in the purification of glycolic acid oxidase.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call