By means of the immunochemical methods of double immuno diffusion and tandem crossed immuno electrophoresis we have compared the bifunctional enzyme RuBP carboxylase/oxygenase from tobacco mutants which differ with respect to their rates of photosynthesis and photorespiration. The comparative studies were carried out with a monospecific antiserum to the enzyme of the wild type Nicotiana tabacum var. John William’s Broadleaf. RuBP carboxylase/oxygenase from the green, yellow-green and yellow phenotype of the mutants namely N. tabacum Su/su, N. tabacum Su/su var. Aurea, N. tabacum var. Consolation, N. tabacum var. NC 95 and N. tabacum Xanthi (D 523) are immunochemical^ identical to the enzyme of the wild type N. tabacum var. John William’s Broadleaf. Furthermore, immunochemical identity of the RuBP carboxylase/oxygenase exists between Nicotiana tabacum and other representatives of the Solanaceae such as Solanum tuberosum, S. lycopersicum and Datura suaveolens. In contrast to this only partial identity to the enzymes of the C3-plants Antirrhinum majus, Spinacia oleracea, Sinapsis alba, Petroselinum crispum, Allium porrum, Hordeum vulgare, Avena sativa to the enzymes of the green alga Chlorella vulgaris and to the blue-green alga Oscillatoria chalybea as well as to the enzyme of the C4-plant Zea mays is observed.
Acclimation of wild-type cells and CO2-insensitive mutants of the green alga Chlorella ellipsoidea to elevated [CO2]