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Plant Physiology 58:135-139 (1976)
© 1976 American Society of Plant Biologists

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Articles

Light Modulation of Glucose-6-Phosphate Dehydrogenase

Partial Characterization of the Light Inactivation System and its Effects on the Properties of the Chloroplastic and Cytoplasmic Forms of the Enzyme 1

Louise E. Anderson2 and Jeffrey X. Duggan

a Department of Biological Sciences, University of Illinois at Chicago Circle, Chicago, Illinois 60680

Light inactivation of glucose-6-phosphate dehydrogenase within the pea (Pisum sativum L.) leaf chloroplast has a narrow pH optimum between 7.2 and 7.4 and is NADP-sensitive. The pH optimum for dark activation is slightly lower. Inactivation apparently results in a simple decrease in maximal velocity of the chloroplastic and cytoplasmic forms of the enzyme with no concomitant change in pH optimum or Km (glucose 6-phosphate).


2 To whom reprint requests should be addressed.

1 This work was supported by National Science Foundation Grant BMS 75-02281.




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J. Biol. Chem.Home page
I. Wenderoth, R. Scheibe, and A. von Schaewen
Identification of the Cysteine Residues Involved in Redox Modification of Plant Plastidic Glucose-6-phosphate Dehydrogenase
J. Biol. Chem., October 24, 1997; 272(43): 26985 - 26990.
[Abstract] [Full Text] [PDF]




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Copyright © 1976 by the American Society of Plant Biologists