Stimulation of the Synthesis of Fructose 1,6-Diphosphate Aldolase by Transferrin
The glycolytic enzyme aldolase (E.C.188.8.131.52) 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).
KeywordsStandard Culture Medium Glycolytic Enzyme Myogenic Cell Breast Muscle Dystrophic Muscle
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