Abstract.
Membrane preparations from suspension-cultured cells of French bean (Phaseolus vulgaris L.) contained callose synthase (EC 2.4.1.34) activity which was preserved upon solubilisation. Following elicitor treatment of cell cultures, increased activity could be extracted and this increase was maintained during purification. The enzyme was purified by high-pressure liquid chromatography and active fractions showed a variable association of two polypeptides of relative molecular masses (Mr) 55 000 and 65 000, the latter being in excess. The Mr-65 000 polypeptide was purified to homogeneity and an antibody raised to it. This antibody showed complex effects on callose synthase activity when incubated with membrane and soluble extracts. In comparison with other systems, the Mr-55 000 subunit is likely to represent the catalytic subunit while the Mr-65 000 polypeptide is a possible regulatory subunit. The Mr-65 000 polypeptide was immunolocated in membranes at sites of callose synthesis in the plant, in cell plates, in sieve plates, at the plasma membrane-wall interface of wounded cells and in papillae in infected cells.
Similar content being viewed by others
Author information
Authors and Affiliations
Additional information
Received: 18 January 1997 / Accepted: 8 May 1997
Rights and permissions
About this article
Cite this article
McCormack, B., Gregory, A., Kerry, M. et al. Purification of an elicitor-induced glucan synthase (callose synthase) from suspension cultures of French bean (Phaseolus vulgaris L.): purification and immunolocation of a probable Mr-65 000 subunit of the enzyme. Planta 203, 196–203 (1997). https://doi.org/10.1007/s004250050182
Issue Date:
DOI: https://doi.org/10.1007/s004250050182