Plant Physiol. Illumina
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Plant Physiology 65:897-901 (1980)
© 1980 American Society of Plant Biologists

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Articles

Glyceraldehyde-3-Phosphate Dehydrogenase in Greening Zea mays L. Leaves 1

Chin Ho Lin2 and C. Ralph Stocking

Department of Botany, University of California, Davis, California 95616

Nicotinamide adenine dinucleotide phosphate (NADP)-dependent glyceraldehyde-3-phosphate dehydrogenase (GPDH) (EC 1.2.1.13), a chloroplast enzyme, had low activity in etioplasts of maize leaves. A light dependent increase of enzyme activity of 7-day-old etiolated seedlings showed a lag period of about 2.5 hours followed by a rapid increase in activity during the next 10 hours. The chlorophyll content followed a similar pattern of increasing concentration, but its formation was not directly related to NADP-GPDH formation. The specific activity of NADP-GPDH was lowest in the morphologically youngest tissue near the base of the lamina. The increase in NADP-GPDH was inhibited by cycloheximide but not by chloramphenicol. This indicates that at least some of the enzyme polypeptides are synthesized by 80S ribosomes in the cytoplasm, transported into chloroplasts and become active in chloroplasts. In etiolated maize shoots subjected to a combination of both 3-(p-chlorophenyl)-1,1-dimethylurea, monuron at 7 x 10–5M and far red light treatment for 15 hours, the NADP-GPDH activity increased 42% over the dark control compared to 70% increase for the light control. It is concluded that NADPH is not absolutely required for the activation of NADP-GPDH in maize leaves under physiological conditions.

2 Present address: Department of Botany, National Chung Hsing University, Taichung, Taiwan.

1 This research was supported in part by National Science Foundation Grants BMS 72-02274 AOZ and PCM 77-12546.






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ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1980 by the American Society of Plant Biologists