Add time:08/30/2019         Source:sciencedirect.com

This study aims at clarifying the cause of the time-dependent, partial loss of the activity during reaction, fallover, of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) of plant sources. This was done by comparing the reaction courses calculated using the reaction models constructed here based on the present conflicting two ideas on fallover with directly measured courses with RuBisCO purified from spinach leaves. Calculation with a model assuming the binding of xylulose 1,5-bisphosphate (XuBP) to the catalytic sites of the enzyme as the cause of fallover and using the reported dissociation constant of XuBP in the binding and the reported rate of the formation of XuBP from ribulose 1,5-bisphosphate (RuBP) gave a rather linear reaction course. The model constructed assuming that hysteresis was the cause of fallover could calculate the measured reaction courses for the initial 20 minutes of reaction at both 0.5 and 2 milimolar RuBP. The rate constants of the hysteretic conformational changes of the predicted enzyme forms to others were given.

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