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Previously, it was reported that plant protoplasts isolated from  Betula platyphylla  (white birch) callus secreted bundles of hollow callose fibrils in acidic culture medium containing a high concentration of calcium ions (Ca 2+ ). Here, the callose synthase was characterized from  in situ  and  in vitro  perspectives. Localization of callose synthases at the secreting site of callose fiber was indicated from  in situ  immunostaining observation of protoplasts. For  in vitro  analyses, membrane proteins were extracted from membrane fraction of protoplasts with a 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) treatment. The CHAPS extract aggregated in the presence of a high concentration of Ca 2+ , suggesting that Ca 2+  may promote the arrangement of callose synthases in the plasma membrane. The callose synthase activity was dependent on pH and Ca 2+ , similar to the callose synthase of  Arabidopsis thaliana . However, the synthesized fibril products were longer than those produced by callose synthases of herbaceous plants. This is the first insight into the specific properties of callose synthases of woody plants that secrete of callose hollow fibers.

holzforschung

Callose-synthesizing enzymes as membrane proteins of  Betula  protoplasts secrete bundles of β-1,3-glucan hollow fibrils under Ca 2+ -rich and acidic culture conditions