01944nam a2200253Ia 4500003001000000005001700010040000900027245018500036490006100221520098600282650003801268650001501306650002901321650000801350650001901358700001801377700002601395700002001421700001501441700001801456700001901474856015601493008004101649MX-MdCICY20260521091450.0  cCICY10aStimulation of Ribulose Bisphosphate Carboxylase Activity by Inorganic Orthophosphate without an Increase in Bound Activating CO2: Co-operativity between the Subunits of the Enzyme0 vJournal of Experimental Botany, 36(9), p.1396-1404, 19853 aRibulose bisphosphate carboxylase/oxygenase (E.C. 4.1.1.39)from wheat (Triticum aestivum L.), already activated by reaction with CO2 and Mg2+, was increased in activity on addition of inorganic orthophosphate. This further activation took place without a significant increase in the amount of bound activating CO2 and the effect was relatively greater with smaller amounts of bound CO2. With less than 2-0 mol of CO2 bound per mol holoenzyme, phosphate increased activity about five-fold whilst with 70 mol of bound activating CO2 per mol holoenzyme, phosphate increased activity by a factor of only 1 -8. This decrease in the effect of orthophosphate with increase in bound activating CO2 suggests negative co-operativity between activated sites. The stimulation of activity by inorganic orthophosphate must be a process distinct from activation by CO2; it was observed with both the slow and the rapidly activating forms of ribulose bisphosphate carboxylase/oxygenase from wheat.14aRIBULOSE BISPHOSPHATE CARBOXYLASE14aACTIVATION14aINORGANIC ORTHOPHOSPHATE14aCO214aCO-OPERATIVITY12aParry, M.A.J.12aGodfrey Schmidt, C.N.12aCornelius, M.J.12aKeys, A.J.12aMillard, B.N.12aGutteridge, S.40uhttps://drive.google.com/file/d/1i_HuWPZYLc2SPAu0tU6YRNj9Bn3jKZav/view?usp=drivesdkzPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx250602s9999    xx |||||s2   |||| ||und|d