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Stoichiometry in the assay of ribulose bisphosphate oxygenase and carboxylase

โœ Scribed by K. Purohit; B.A. McFadden; Ashok Saluja

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
893 KB
Volume
124
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

Complete stoichiometry of the reaction catalyzed by ribulose l$bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25'C in the presence of 1 N NaOH or by complete carboxylation using "C02 and RuBP carboxylase. The RuBP-dependent oxygen consumption has been measured continuously with an oxygen electrode. After termination of catalysis, 3-phosphoglycerate production has been determined spectrophotometrically using phosphoglycerokinase, glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase, Lu-glycerophosphate dehydrogenase, ATP, and NADH. To measure phosphoglycolate, this product was first hydrolyzed with alkaline phosphatase and the resultant glycolate oxidized by glycolate oxidase. Attendant HzO, formation catalyzed by peroxidase has then been measured calorimetrically. Interference by ribulose in the measurement of glycolate can be easily corrected. Procedures are rapid and do not require separation of reactants and products. Results are in excellent accord with the expected stoichiometrv for catalysis bv RuBP oxygenase and also enable an estimate of competing catalysis by RuBP carboxylase. ---

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