GLYCOGEN SYNTHESIS IN MUSCLE LACKING PHOSPHORYLASE

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Abstract
Muscle biopsies have been obtained from normal human subjects and from a patient with a progressive myopathy whose muscles lack phosphorylase. The phosphorylase level in a homogenate of the patient''s muscle was found to be less than 0.5% of normal, while uridine diphosphoglucose (UDPG)-glycogen synthetase was approximately 1/2 of normal. The phosphoglucomutase activity of a homogenate of the patient s muscle was about 1/3 that of controls. The lower UDPG-glycogen synthetase and phosphoglucomutase are interpreted in terms of general degeneration of the tissue, while the lack of phosphorylase is considered to be a specific defect. The phosphorylase kinase activity of the homogenate was normal. The enzymatic pattern and the presence of a high concentration of glycogen in the tissue give strong evidence that glycogen is synthesized by way of UDPG.

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