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Plant and Cell Physiology, 1981, Vol. 22, No. 5 891-898
© 1981

Article

Cell wall Pyrophosphatase from Higher Plants

Emma Nelly Ouiroga1, Teresa Re de Maxud1, Elena Arias de Flores1 and Antonio Rodolfo Sampietro2,3

1Cátedra de Química Biológica, Facultad de Bioquímica, Química y Farmacia, Universidad National de Tucuman Chacabuco 461, 4000.-San Miguel de Tucumán, Argentina
2Cátedra de Fitoquímica, Facultad de Bioquímica, Química y Farmacia, Universidad National de Tucumán Ayacucho 491, 4000.San Miguel de Tucumán, Argentina

An alkaline inorganic pyrophosphatase bound to the cell walls of leaf blades from sugar cane is described. The enzyme could not be removed using buffer solutions of various ionic strengths and pH values. As neither Tween 60 nor sodium borate buffercould remove the enzyme, it appears to be firmly bound to the cell wall. The optimum pH was 8.6 and the pyrophosphatase showed an absolute Mg2+ dependence. According to direct and kinetic determinations, the best Mg2+ : PP1 ratio was 10 : 1. The properties of the enzyme fitted classic Michaelis-Menten kinetics well. Other properties of the enzyme such as substrate and metal ion specificities and effects of temperature and of inhibitors were also determined.

Possible implications of where the enzyme is localized are discussed.

3Carreer Investigator from the Consejo Nacional de Investigaciones Cientificas y Tecnicas, Buenos Aires, Argentina.

(Received April 16, 1981; Accepted June 9, 1981)
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