Purification and characterization of glycogen phosphorylase b from fat body of the silkworm, Bombyx mori

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Abstract

  • 1.

    1. Glycogen phosphorylase b from silkworm pupal fat body has been purified to homogeneity as judged by native and SDS-gel electrophoreses.

  • 2.

    2. The enzyme is a monomeric protein having a mol. wt of approx. 92,000.

  • 3.

    3. The enzyme has an absolute requirement for AMP. The Km for AMP is in a range from 0.4 to 0.6 mM and for the maximum activity 2 mM is required.

  • 4.

    4. Phosphorylase b activity measured as a function of Pi concentration shows positive cooperativity at any level of AMP. When measured as a function of glycogen concentration, however, the enzyme follows normal Michaelis-Menten kinetics.

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