Influence of solutes on the inactivation of glutamine synthetase by endopeptidases

Fröhlich, V; Feller, Urs (June 1987). Influence of solutes on the inactivation of glutamine synthetase by endopeptidases. Experientia, 43(6), p. 660. Birkhäuser Verlag

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Glutamine synthetase (GS) extracted from young wheat leaves (low endopeptidase activity) is relatively stable at pH 7.5 and 30°C, but is rapidly inactivated when extract from senescing wheat leaves (high endopeptidase activity), purified papain or trypsin is added. The inactivation of GS in the presence of endopeptidases can be affected by low molecular weight compounds and pH (e.g. 1 mM ATP stabilized the enzyme). In our work several tested solutes had different influences on GS stability. KCl, sucrose, glycine and alanine had no major effect, whereas GS could be protected from inactivation with MgSO4, MgCl2 and lysine. The protective solutes acted in the same manner in the presence of extract from senescing wheat leaves as well as after adding purified papain or trypsin. We conclude that the results mentioned based on interactions with GS and not with endopepfidases. It must be considered that the stability of various enzymes may be affected in a different manner by the same solutes.

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