Enzymes concerned in the synthesis of glycogen from glucose in the brown adipose tissue

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Abstract
Hexokinase, phosphoglu-comutase and phosphorylase were demonstrated in extracts of the brown adipose tissue of the rat. The phosphoglucomutase of brown adipose tissue required Mg ions for its optimum activity, and was inhibited by NaF and by high concns. of glucose-1-phosphate. The phosphorylase of brown adipose tissue was prepared free from phosphatase and phosphoglucomutase; it was activated by cysteine and glycogen and inhibited by glucose, alpha-methyl-D-glucoside and by phlorrhizin. It was impossible to demonstrate unequivocally whether the phosphorylase in the adipose tissue was in the a or b form since the prepn. obtained might have been contaminated with suboptimal concns. of adenylic acid. Extracts of brown adipose tissue contained prosthetic group removing enzyme. The polysaccharide synthesized by the phosphorylase of brown adipose tissue stained brown with I2 and was assumed to possess a branched structure. Extracts of the brown adipose tissue of the rat contained supplementary enzyme which, in conjunction with phosphorylase a, catalyzed the synthesis from glucose-l-phosphate of a branched polysaccharide similar to glycogen.

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