Properties of acid phosphatase in the cell wall of tobacco cells cultured in vitro

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A cell-wall fraction containing 10.0% dry weight of protein was isolated from tobacco (Nicotiana tabacum L.) XD-6 cells cultured in suspension. The fraction possessed high acid phosphatase activity toward p-nitrophenyl phosphate, phenyl phosphate, inorganic pyrophosphate, adenosine diphosphate, nucleoside triphosphates, and bis-(p-nitrophenyl) phosphate; much less activity toward naphthyl phosphate, β-glycero-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-diphosphate, thiamine pyrophosphate; and no activity toward glucose-1-phosphate and inositol hexaphosphate. Metallic ions were not required for activation. The enzyme was extracted from the wall with NaCl solution. The solubilized enzyme resulted in a single peak on Sephadex G-150 chromatography with activity toward p-nitrophenyl phosphate, pyrophosphate, and bis-(p-nitrophenyl) phosphate. The activity of the solubilized enzyme toward p-nitrophenyl phosphate was identical with the bound enzyme in its pH optimum, substrate specificity, ion inhibition and K_m value, but it was more sensitive to pH, substrate difference, inhibition, and heat treatment.
日本植物生理学会の論文