Plant Physiology 100:1737-1743 (1992)
© 1992 American Society of Plant Biologists
Environmental and Stress Physiology
Distinctive Responses of Ribulose-1,5-Bisphosphate Carboxylase and Carbonic Anhydrase in Wheat Leaves to Nitrogen Nutrition and their Possible Relationships to CO2-Transfer Resistance 1
Amane Makino2,
Hiroshi Sakashita,
Jun Hidema,
Tadahiko Mae,
Kunihiko Ojima and
Barry Osmond3
Department of Botany, Duke University, Durham, North Carolina 27706,
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Tsutsumidori-Amamiyamachi, Sendai 981, Japan
The amounts of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), total chlorophyll (Chl), and total leaf nitrogen were measured in fully expanded, young leaves of wheat (Triticum aestivum L.), rice (Oryza sativa L.), spinach (Spinacia oleracea L.), bean (Phaseolus vulgaris L.), and pea (Pisum sativum L.). In addition, the activities of whole-chain electron transport and carbonic anhydrase were measured. All plants were grown hydroponically at different nitrogen concentrations. Although a greater than proportional increase in Rubisco content relative to leaf nitrogen content and Chl was found with increasing nitrogen supply for rice, spinach, bean, and pea, the ratio of Rubisco to total leaf nitrogen or Chl in wheat was essentially independent of nitrogen treatment. In addition, the ratio of Rubisco to electron transport activities remained constant only in wheat. Nevertheless, gas-exchange analysis showed that the in vivo balance between the capacities of Rubisco and electron transport in wheat, rice, and spinach remained almost constant, irrespective of nitrogen treatment. The in vitro carbonic anhydrase activity in wheat was very low and strongly responsive to increasing nitrogen content. Such a response was not found for the other C3 plants examined, which had 10- to 30-fold higher carbonic anhydrase activity than wheat at any leaf-nitrogen content. These distinctive responses of carbonic anhydrase activity in wheat were discussed in relation to CO2-transfer resistance and the in vivo balance between the capacities of Rubisco and electron transport.
2 Permanent address: Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Tsutsumidori-Amamiyamachi, Sendai 981, Japan.
3 Present address: Research School of Biological Sciences, The Australian National University, GPO Box 475, Canberra, A.C.T. 2601, Australia.
1 Research supported by a Duke University grant to B.O. and Grants-in-Aid for Scientific Research (Nos. 03304004 and 03760042) from the Ministry of Education, Science and Culture, Japan to A.M.
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