The in vitro ribulose-1,5-bisphosphate (RuBP) carboxylase activity per unit of leaf nitrogen was found to be 30% greater in Triticum aestivum than in T. monococcum. This was due to a higher specific activity of the enzyme from T. aestivum, as the amount of RuBP carboxylase protein per unit of total leaf nitrogen did not differ between the genotypes. The occurrence of higher specific activity of RuBP carboxylase is shown to correlate with possession of the large subunit derived from the B genome of wheat.Despite the greater RuBP carboxylase activity per unit of leaf nitrogen in T. aestivum, the initial slopes of curves relating rate of CO(2) assimilation to intercellular p(CO(2)) are similar in T. aestivum and T. monococcum for the same nitrogen content per unit leaf area. The similarity of the initial slopes is the result of a greater resistance to CO(2) transfer between the intercellular spaces and the site of carboxylation in T. aestivum than in T. monococcum.
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