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Plant Physiology 64:876-879 (1979)
© 1979 American Society of Plant Biologists

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Articles

Measurement of Ribulose 1,5-Bisphosphate from Spinach Chloroplasts 1

Richard C. Sicher, James T. Bahr2 and Richard G. Jensen

a Departments of Biochemistry and Plant Sciences, University of Arizona, Tucson, Arizona 85721

A technique has been developed for the rapid and simple measurement of ribulose 1,5-bisphosphate from isolated spinach chloroplasts. The endogenous ribulose bisphosphate was detected enzymically using 14CO2 and ribulose bisphosphate carboxylase/oxygenase released from the chloroplasts. Ribulose 5-phosphate kinase was inhibited with 0.4 to 0.6 millimolar 2,6-dichlorophenol-indophenol and 4 micromolar carbonyl cyanide m-chlorophenylhydrazone. Phosphoenolpyruvate carboxylase activity was low with washed chloroplasts and its labeled product, [14C]oxalacetate, was destroyed by heating with 1.0 N HCl at 90 C. The assay method was linear from 0.05 to 0.87 nanomoles ribulose bisphosphate per milliliter. The latter value was determined with chloroplast material having 44 micrograms of chlorophyll per milliliter. This technique was simple and direct, used less chloroplast material, yet provided results comparable to a previously described enzymic technique in which ribulose bisphosphate was determined after the precipitation of chloroplast proteins by perchloric acid.

2 Current address: Mobil Chemical Company, P.O. Box 240, Edison, New Jersey 08817.

1 This work was supported by National Science Foundation Grant PCM 75-23240 to RGJ. This is University of Arizona Agricultural Experiment Station Paper 3025.






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Copyright © 1979 by the American Society of Plant Biologists