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- W1993059808 abstract "Activities of ribulose-1,5-bisphosphate carboxylase (rubisco), phosphoenolpyruvate carboxylase (PEPC), aspartate aminotransferase, alanine aminotransferase, NADH-malate dehydrogenase, NADPH-malate dehydrogenase, NAD-malic enzyme, NADP-malic enzyme, and pyruvate phosphate dikinase (PPDK) were measured in leaf extracts of Flaveria cronquistii (C3), F. pubescens, F. anomala (C3−C4), F. brownii, F. palmeri, F. trinervia, and F. australasica (C4). The two C3−C4 intermediate species show activities of PEPC, both aminotransferases, NADPH-malate dehydrogenase, NADP-malic enzyme, and PPDK intermediate between those of C3 and C4 Flaveria species. The Km values of rubisco for CO2 exhibit distinct differences with higher values for the C4 species. PPDK is light activated reaching its maximum activity at noon in F. brownii and, in contrast, very early after the beginning of the light phase in F. pubescens. PEPC from both F. palmeri, F. trinervia, and F. australasica is activated about twofold by NADH but there is no effect to the enzyme of all other Flaveria species. This activation might be a more general feature of PEPC from NADP-malic enzyme type C4 plants. An immunofluorescence investigation of the intercellular compartmentation of rubisco revealed an intermediate distribution of this enzyme in leaves of F. pubescens and F. anomala. Typical immunofluorescence patterns with nearly exclusive localization of rubisco in the mesophyll or bundle sheath cell chloroplasts, respectively, were found in the C3 and C4Flaveria species. The data are discussed with respect to the evolution of C4 photosynthesis from C3 photosynthesis via C3−C4 intermediate types of photosynthetic carbon assimilation." @default.
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- W1993059808 date "1984-01-01" @default.
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- W1993059808 title "Photosynthetic enzyme activities and immunofluorescence studies on the localization of ribulose-1,5-bisphosphate carboxylase/oxygenase in leaves of C3, C4, and C3−C4 intermediate species of Flaveria (Asteraceae)" @default.
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- W1993059808 doi "https://doi.org/10.1016/s0015-3796(84)80041-4" @default.
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