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Ionic control of acid phosphatase activity in plant cell walls
Author(s) -
NOAT GEORGES,
CRASNIER MARTINE,
RICARD JACQUES
Publication year - 1980
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/1365-3040.ep11581782
Subject(s) - ionic strength , chemistry , enzyme , substrate (aquarium) , electrolyte , ionic bonding , ion , phosphate , phosphatase , cell wall , acid phosphatase , inorganic chemistry , biochemistry , organic chemistry , electrode , aqueous solution , biology , ecology
. Purified acid phosphatase from sycamore cell walls is not activated by increasing the ionic strength of the reaction mixture. However activation occurs when the enzyme is bound to small cell wall fragments. The apparent activation of the bound enzyme by ions is paralleled by a decline of the substrate concentration C 1/2 , that results in half of the maximum rate. Above ionic strengths of about 0.05 the bound and solubilized enzyme forms behave in the same manner. Titration of cell wall fragments at different ionic strengths show that the local pH, inside the cell wall fragments, is lower than the pH in bulk solution. These results are explained in the light of poly‐electrolyte theory. The negative charges of the cell walls generate an electrostatic potential that results in the attraction or repulsion of ions. The local concentration of organic phosphate (the substrate of the enzyme) is then lower than its concentration in bulk solution. This concentration difference explains that the value of C 1/2 , or of the apparent K m of the bound enzyme, is greater than the true K m of the solubilized enzyme. Increasing the ionic strength tends to equalize bulk and local ion concentrations, and therefore apparently activates the bound enzyme.