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SUMMARY: Mutants deficient in branching-enzyme activity (glgB) were isolated and classified into four groups. They accumulated different amounts of a linear polysaccharide similar to amylose. The polysaccharides were extracted and purified. Some of their properties were similar, but gel filtration on Agarose fractionated them into three peaks whose size seemed to be related to α-amylase activity. Electron microscopy showed that amylose formed inclusions of varying density and small separated granules; the proportions of these types of aggregates varied from one mutant to another. Amylase deficiency and the glgC mutation (altered ADP-glucose pyrophosphorylase) are important factors in amylose accumulation and aggregation.
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