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Gibbons , R. J. (Forsyth Dental Center, Boston Mass.). Metabolism of intracellular polysaccharide byStreptococcus mitis and its relation to inducible enzyme formation. J. Bacteriol.87: 1512–1520. 1964.—The synthesis and catabolism of an intracellular iodine staining polysaccharide produced from glucose byStreptococcus mitis was investigated. Approximately 15% of the total glucose metabolized by buffered suspensions ofS. mitis was assimilated. Over 90% of the assimilated glucose was converted into a polysaccharide of the glycogen-amylopectin type. Use of uniformly labeled C14 -glucose provided a convenient method for determining polysaccharide accumulation in this organism. Glucose assimilation occurred at a rate of over 80 μg of glucose per hr per 100 μg of starting dry cell weight. Prolonged assimilation produced cells containing over 50% polysaccharide on a dry weight basis. Accumulated polysaccharide was catabolized at the same rate when the organism was suspended in buffer, sugar-free broth, or sugar-free broth containing thiomethyl galactoside. Metabolic intermediates produced from polysaccharide catabolism did not markedly repress inducible enzyme synthesis. The last glucose molecules incorporated into polysaccharide were among the first molecules to be removed during catabolism. Catabolism of polysaccharide providesS. mitis with energy in a utilizable form, for cells containing polysaccharide increased in β-galactosidase activity when induced with thiomethyl galactoside in the absence of an exogenous energy source. Cells devoid of polysaccharide, and a polysaccharide-negative variant ofS. mitis did not increase in β-galactosidase activity when induced in a similar manner. It appears that the intracellular polysaccharide is the sole substrate for the endogenous metabolism ofS. mitis .

METABOLISM OF INTRACELLULAR POLYSACCHARIDE BY STREPTOCOCCUS MITIS AND ITS RELATION TO INDUCIBLE ENZYME FORMATION