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Related Experiment Videos

L-type glycogen synthase. Tissue distribution and electrophoretic mobility.

H R Kaslow, D D Lesikar, D Antwi

    The Journal of Biological Chemistry
    |August 25, 1985
    PubMed
    Summary

    This study identifies two distinct forms of glycogen synthase: M-type in muscle and L-type in liver. These isozymes exhibit different tissue distributions and molecular weights, indicating structural variations between muscle and liver glycogen synthase.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Previous work identified antisera against rat skeletal muscle glycogen synthase, suggesting tissue-specific isozymes.
    • These antisera recognized a skeletal muscle-type (M-type) glycogen synthase in various rat tissues, excluding the liver.

    Purpose of the Study:

    • To investigate the distribution and electrophoretic properties of liver-specific glycogen synthase (L-type).
    • To compare the structural characteristics of M-type and L-type glycogen synthase.

    Main Methods:

    • Immunoblot analysis using antisera specific for rat L-type and M-type glycogen synthase.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to determine electrophoretic mobility.
    • Analysis of crude tissue extracts and purified enzymes from rat and rabbit.

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    Main Results:

    • L-type glycogen synthase was exclusively found in rat liver, while M-type was present in other tissues but not liver.
    • Rat L-type synthase had an apparent molecular mass (Mapp) of 85,000, distinct from M-type synthase (Mapp = 86,000 and 89,000).
    • Proteolysis of L-type synthase generated smaller forms (Mapp = 75,000), and cross-species comparisons revealed structural differences between rat and rabbit glycogen synthases.

    Conclusions:

    • Rat liver and skeletal muscle possess distinct glycogen synthase isozymes (L-type and M-type, respectively).
    • These isozymes differ in tissue distribution and molecular structure.
    • Structural differences are inherent to the proteins and not due to bound factors.