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Structural studies on rabbit muscle glycogen synthase. I. Subunit composition

Y Takeda, H B Brewer, J Larner

    The Journal of Biological Chemistry
    |December 10, 1975
    PubMed
    Summary

    Rabbit muscle glycogen synthase I and D forms were purified, revealing distinct subunit compositions and oligomeric states. Proteolysis affects the I form

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Glycogen synthase exists in two interconvertible forms, I (independent of glucose-6-phosphate) and D (dependent).
    • Understanding the structural differences between these forms is crucial for elucidating glycogen metabolism regulation.

    Purpose of the Study:

    • To purify and characterize the rabbit muscle glycogen synthase I and D forms.
    • To investigate the subunit composition, molecular weight, and oligomeric states of both enzyme forms.

    Main Methods:

    • Enzyme purification to high specific activity.
    • Polyacrylamide gel electrophoresis (SDS-PAGE and native PAGE).
    • Peptide mapping via 2D chromatography and high-voltage electrophoresis.
    • N-terminal amino acid sequencing (Edman degradation).

    Main Results:

    • Purified synthase I and D forms exhibited high specific activity.
    • SDS-PAGE revealed distinct subunit molecular weights for I (85,000 and 81,000 Da) and D (85,000 Da) forms.
    • The 81,000 Da subunit of the I form is a proteolysis product.
    • Peptide mapping confirmed subunit molecular weights.
    • N-terminal sequencing identified Pro-Leu- as the start of the D form and Pro-Leu-Ser-Ser-Thr-Leu-Ser-Val- for the I form.
    • Native PAGE showed I form as dimer/tetramer and D form as trimer/tetramer.

    Conclusions:

    • Rabbit muscle glycogen synthase I and D forms possess different subunit compositions and oligomeric structures.
    • Proteolytic modification impacts the subunit composition of the I form.
    • These structural differences likely contribute to the distinct enzymatic properties and regulation of the I and D forms.

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