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. 1987 Sep;85(1):131–136. doi: 10.1104/pp.85.1.131

Modulation of Pea Membrane β-Glucan Synthase Activity by Calcium, Polycation, Endogenous Protease, and Protease Inhibitor 1

Vincent Girard 1,2, Gordon Maclachlan 1
PMCID: PMC1054217  PMID: 16665644

Abstract

β-Glucan synthase activity in plant membranes can be markedly altered by a multiplicity of apparently unrelated factors. In pea epicotyl membranes it is enhanced by low and inhibited by high concentrations of added Ca2+, trypsin or soluble pea protease. Ca2+ stimulates preexisting synthase activity, particularly in the presence of polycations (spermidine), but protease treatments activate and, with time, inactivate synthase zymogen. Endogenous pea protease activity is also associated with washed pea membrane and appears to be responsible for the decay observed with time in the β-glucan synthase activity. Endogenous pea protease activity is inhibited by thiol inhibitors, e.g. iodoacetamide and Hg2+, and by a heat-stable peptide, molecular weight approximately 10,000, that is found in supernatants of pea extracts. These protease inhibitors have the capacity to protect β-glucan synthase activity from denaturation or its zymogen from activation due to endogenous or added protease activity. Evidence is described which supports the proposal that 1,4-β-glucan synthase is destroyed and possibly converted to 1,3-β-glucan synthase activity by protease action, and that the latter may then be greatly enhanced by Ca2+ and polycations.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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