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Stimulation of the Synthesis of Fructose 1,6-Diphosphate Aldolase by Transferrin

  • T. H. Oh
  • G. J. Markelonis
  • T. Dion Guidera
  • S. L. Hobbs
  • L. P. Park
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 182)

Abstract

The glycolytic enzyme aldolase (E.C.4.1.2.13) catalyzes the reversible cleavage of fructose 1,6-diphosphate to yield dihydorxyacetone phosphate and D-glyceraldehyde 3-phosphate. During embryonic development in skeletal muscle, this tetrameric enzyme undergoes a transition from a macromolecule composed primarily of C subunits to a homotetramer composed of A subunits (332–334). The work of Lebherz has shown that the steady-state concentration of aldolase and other glycolytic enzymes in “fast” and “slow-twitch” skeletal muscle fibers is regulated almost solely at the level of protein synthesis (334,335). During post-embryonic development, the synthetic rate of aldolase becomes four-fold faster in “fast-twitch” chicken breast muscle as compared to “slow-twitch” leg muscle (334–336). Thus, in terms of the glycolytic enzymes, fiber-type differentiation appears to progress via a transformation from a slow-type phenotype to a fast-type (335).

Keywords

Standard Culture Medium Glycolytic Enzyme Myogenic Cell Breast Muscle Dystrophic Muscle 
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

© Plenum Press, New York 1985

Authors and Affiliations

  • T. H. Oh
    • 1
  • G. J. Markelonis
    • 1
  • T. Dion Guidera
    • 1
  • S. L. Hobbs
    • 1
  • L. P. Park
    • 1
  1. 1.Department of AnatomyUniversity of Maryland School of MedicineBaltimoreUSA

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