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Plant Physiology 50:446-451 (1972)
© 1972 American Society of Plant Biologists

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The Activity of Ribulose Diphosphate Carboxylase in Extracts of Gonyaulax polyedra in the Day and the Night Phases of the Circadian Rhythm of Photosynthesis 1

Karen J. Bush2 and Beatrice M. Sweeney

a Department of Biological Sciences, University of California, Santa Barbara, California 93106

The ribulose 1,5-diphosphate carboxylase from Gonyaulax polyedra Stein. has a half-life of about four hours in buffer, but can be stabilized by the addition of 50% glycerol. The optimum pH is 7.8 to 8.0 and the optimum Mg2+ concentration is 3 mM. Heavy metal ions (Cu2+, Hg2+, Ni2+, Zn2+), EDTA, pyrophosphate, and adenosine triphosphate were strongly inhibitory. Ribulose 1,5-diphosphate carboxylase from Gonyaulax was not cold-sensitive or activated by light activation factor from tomato or Gonyaulax. No difference in the activity of this enzyme was detected when extracts prepared at the maximum and the minimum of the circadian rhythm of photosynthesis were compared. The Km of HCO3– was also the same (16 to 19 mM).

2 Present address: Department of Biochemistry, School of Medicine, The University of North Carolina, Chapel Hill, N. C. 27514.

1 This research was supported in part by Grant GB 8418 from the National Science Foundation.




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N. Nassoury, L. Fritz, and D. Morse
Circadian Changes in Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Distribution Inside Individual Chloroplasts Can Account for the Rhythm in Dinoflagellate Carbon Fixation
PLANT CELL, April 1, 2001; 13(4): 923 - 934.
[Abstract] [Full Text]


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