beta-Glucan synthases were solubilized by treating membrane preparations from suspension-cultured ryegrass (lolium multiflorum) endosperm cells with detergents. Of the seven detergents tested only digitonin and octyl glucoside dissociated active synthases from the membranes. The digitonin-solubilized enzymes produced 1,4-beta-glucans and 1,3:1,4-beta-glucans, whereas the digitonin-insoluble enzymes produced, in addition, 1,3-beta-glucans. Chromatography of the digitonin-solubilized beta-glucan synthases on DEAE-Sepharose resulted in their partial purification. The octyl glucoside-solubilized enzymes produced more 1,3-beta-glucans than did the membrane-bound preparations. These results suggest that the 1,3-beta-glucan synthase is a separate enzyme and is not involved in 1,3:1,4-beta-glucan synthesis. Digitonin not only dissociated synthases from the membranes, but also stimulated synthase activity. This effect may be related to the inhibition by digitonin of glucosyl transfer from UDP-glucose to form steryl glucosides.
Research Article| June 01 1982
Solubilization of β-glucan synthases from the membranes of cultured ryegrass endosperm cells
Biochem J (1982) 203 (3): 629–636.
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R J Henry, B A Stone; Solubilization of β-glucan synthases from the membranes of cultured ryegrass endosperm cells. Biochem J 1 June 1982; 203 (3): 629–636. doi: https://doi.org/10.1042/bj2030629
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