酵母のグリコーゲン代謝におけるグリコーゲンの構造とPhosphorylaseおよびDebranching酵素の関係

概要

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The changes of glycogen structure and activities of phosphorylase and amylo-1,6-glucosidase/oligo-1,4→1,4-glucan transferase (glucosidase/transferase) of a strain (5002-5C) of Aaccharomyces cerevisiae, which is capable of accumulating large amounts of glycogen, were examined under starving and feeding of glucose and the following results were obtained.I. The average chain length and the limit of β-amylolysis of the glycogen at the late logarithmic phase were 18.1 and 57.9%, respectively. These values suggest that the glycogen has larger outer chains than that of a normal strain of Saccharomyces and a similar structure to amylopectin.II. When cells in the late logarithmic phase were transfereed to a glucose-starving medium, the phosphorylase activity increased rapidly and both the content and the average chain length of glycogen decreased. When the cells were transferred back to a glucose-containing medium they rapidly reverted to the original values. However, the glucosidase/transferase did not change under these conditions.These results suggest that the phosphorylase activity in regulated by physiological conditions and plays an important role in the regulation of glycogen degradation but that the debranching enzyme controls the rate-limiting step in the degradation.
社団法人日本生物工学会の論文
1978-03-25