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THE KINETICS OF THE ENZYMATIC SYNTHESIS OF GLYCOGEN FROM GLUCOSE-1-PHOSPHATE
Open accessAbstract
The reversible enzymatic reaction, glycogen + inorganic phosphate F? glucose-l-phosphate, is of unusual interest, since it is the first known case of an in vitro synthesis of a polysaccharide of high molecular weight. In the following pages the kinetics of this reaction are described in some detail; its physiological significance has been discussed in recent articles (1). When the reaction, catalyzed by the enzyme phosphorylase, proceeds to the left, inorganic phosphate is formed which may be determined by the method of Fiske and Subbarow (2), with the Summerson (3) photoelectric calorimeter. This offers a convenient means of studying the reaction. The amount of polysaccharide formed agrees well with the value calculated from the inorganic phosphate liberated (4) .1 Phosphorylase was prepared from mammalian skeletal muscle, heart, brain, and liver. The method of purification of the enzyme was the same as outlined previously (4) but several improvements were introduced which will be described in a later publication. Substrate Concentration-The curve expressing the relation
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Cited by
CRYSTALLINE MUSCLE PHOSPHORYLASE
Green, A. A., & Cori, G. T. (1943) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)72110-8 · Cited by 314
Self-citationKobayashi, S., & Uyama, H. (2003) · Encyclopedia of Polymer Science and Technology · doi:10.1002/0471440264.pst118 · Cited by 13
Metadata
- Authors
- Cori, G. T., & Cori, C. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1940-09
- Volume
- 135
- Issue
- 2
- Pages
- 733-756
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W201536040
- Cited by
- 173
- References
- 0
- FWCI
- 6.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Cori, G. T., & Cori, C. F. (1940). THE KINETICS OF THE ENZYMATIC SYNTHESIS OF GLYCOGEN FROM GLUCOSE-1-PHOSPHATE. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)73136-0
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