Ribulose 1,5-bisphosphate carboxylase/oxygenase from citrus leaves
Identifieur interne : 004355 ( Main/Merge ); précédent : 004354; suivant : 004356Ribulose 1,5-bisphosphate carboxylase/oxygenase from citrus leaves
Auteurs : Lola Pe Arrubia [Espagne] ; Joaquín Moreno [Espagne]Source :
- Phytochemistry [ 0031-9422 ] ; 1988.
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase was purified to homogeneity from citrus leaves. Decreases of the carboxylase specific activity was observed throughout the purification process. Inactivation and loss of the enzyme occurred through shear involving manipulations, but these effects could be minimized using a high fresh material/extraction volume ratio and protective agents such as non-ionic detergents, urea and bovine serum albumin. The enzyme had a S20,w = 19.4 S and a Mr of ca 520 000, with subunits of 50 000 and 15 500. The holoenzyme dissociated spontaneously into its subunits at pH values between 3.5 and 5.5 with precipitation of the large subunit and leaving most of the small one in solution. The citrus carboxylase showed unusual kinetic features such as a high (0.34 mM) Km(RuBP) and a low (7.6) pH optimum. Km(CO2) was 21 μM. The carboxylase activity was strongly inhibited by ionic strengths higher than 0.1 M.
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DOI: 10.1016/0031-9422(88)80085-2
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