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Regulation of Muscle Glycogenolysis

  • Ronald D. Edstrom
  • Marilyn H. Meinke
  • Mary E. Gurnack
  • David M. Steinhorn
  • Xiuru Yang
  • Rui Yang
  • D. Fennell Evans
Chapter
Part of the NATO ASI Series book series (NSSA, volume 190)

Abstract

During muscle contraction, a significant part of the energy used is derived from glycogen. The rate of glucose 1-phosphate production from glycogen is determined by the fraction of glycogen phosphorylase in the phosphorylated, active, a form (Madsen, 1986). The fractions of phosphorylase in the a and b (dephospho-, inactive) forms depend on the two enzymes, phosphorylase kinase and protein phosphatase-1, which in turn are influenced by other enzymes and regulatory factors, all of which form an integrated, multienzyme glycogenolytic complex (Fig. 1) (Hallenbeck & Walsh, 1986). In this report we describe three experimental approaches to the study of regulation of this complex.

Keywords

Scanning Tunnelling Microscopy Glycogen Phosphorylase Glycogen Particle Phosphorylase Kinase Linear Aggregate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Ronald D. Edstrom
    • 1
  • Marilyn H. Meinke
    • 1
  • Mary E. Gurnack
    • 1
  • David M. Steinhorn
    • 2
  • Xiuru Yang
    • 3
  • Rui Yang
    • 3
  • D. Fennell Evans
    • 3
  1. 1.Department of BiochemistryUniversity of MinnesotaMinneapolisUSA
  2. 2.Department of PediatricsUniversity of MinnesotaMinneapolisUSA
  3. 3.Center for Interfacial EngineeringUniversity of MinnesotaMinneapolisUSA

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