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Plant and Cell Physiology, 1977, Vol. 18, No. 3 693-699
© 1977

Short communication

Ribulose-1,5-bisphosphate carboxylase from plants adapted to extreme environments

D.J. Weber, William R. Andersen, Samuel Hess, D.J. Hansen and M. Gunasekaran

Department of Botany and Range Science, Brigham Young University Provo, Utah 84602, U.S.A.

The Km and Vmax of ribulose-1,5-bisphosphate carboxylase (RuBPCase) in selenium absorbing plants (Astragalus flavus Barn., Astragalus rafaelensis Barn. and Stanleya pinnata Bril.) were similar to RuBPCase from tomato (Lycopersicon esculentum L. var. tropic). The pH optima for RuBPCase activity was 8.0 for L. esculentum and A. flavus and 7.0 for A. rafaelensis and S. pinnata. The Activation Energy ({delta}E) values for the enzymes were as follows: A.flavus (21.37), S.pinnata (19.85), A. rafaelensis (19.12) and L. escudentum (18.58). The energy of activation was higher for the desert plants as compared to the tomato. The Arrhenius plot curves were linear to 50°C far the desert plants as compared to 45°C for tomato.

Enzyme kinetics of RuBPCase from halophytic plants (Salicornia pacifica Stand., var. utahensis (Tidestrom) Munz. and Salicornia rubra Nels.) indicated the enzyme was at least as sensitive to NaCl concentrations as the enzyme from tomato.

(Received November 9, 1976; )
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