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J Bacteriol. 1973 February; 113(2): 946-952
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Purification and Properties of the Adenosine Diphosphoglucose:Glycogen Transglucosylase of Pasteurella pseudotuberculosis

D. N. Dietzler1 and J. L. Strominger

a Department of Biochemistry and Molecular Biology, Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138

ABSTRACT

The enzyme which catalyzes the transfer of glucosyl residues from adenosine diphospho(ADP)-glucose to glycogen has been partially purified from extracts of Pasteurella pseudotuberculosis. In contrast to other glycogen synthetases of this type, guanosine diphospho-glucose had about 5% of the activity of ADP-glucose as a glucosyl donor. Some other properties of the enzyme are described and compared to other bacterial glycogen synthetases.


FOOTNOTES

1 Present address: Department of Pediatrics, Washington University School of Medicine, St. Louis, Mo. 63110.


J Bacteriol. 1973 February; 113(2): 946-952
Copyright © 1973 American Society for Microbiology. All Rights Reserved.







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