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

@article{Morishima1985PurificationAC,
  title={Purification and characterization of glycogen phosphorylase b from fat body of the silkworm, Bombyx mori},
  author={I. Morishima and S. Sakurai},
  journal={Comparative Biochemistry and Physiology B},
  year={1985},
  volume={81},
  pages={453-458}
}
  • I. Morishima, S. Sakurai
  • Published 1985
  • Biology
  • Comparative Biochemistry and Physiology B
  • 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 K m 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 P i concentration shows positive cooperativity at any level of… CONTINUE READING
    10 Citations
    Purification and characterization of glycogen phosphorylase A and B from the freeze-avoiding gall moth larvae Epiblema scudderiana
    • 6
    • Highly Influenced
    Allosteric effectors and trehalose protect larval Manduca sexta fat body glycogen phosphorylase B against thermal denaturation.
    • 11
    • PDF
    Structural and functional properties of Drosophila melanogaster phosphorylase: comparison with the rabbit skeletal muscle enzyme.
    • 8
    Molecular cloning and seasonal expression of oyster glycogen phosphorylase and glycogen synthase genes.
    • H. Bacca, A. Huvet, +5 authors J. Moal
    • Biology, Medicine
    • Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
    • 2005
    • 64
    • PDF
    Molecular cloning and seasonal expression of oyster glycogen phosphorylase and glycogen synthase genes

    References

    SHOWING 1-10 OF 18 REFERENCES
    GLYCOGEN PHOSPHORYLASE AND ITS ACTIVATION IN SILKMOTH FAT BODY.
    • 49
    COMPARATIVE STUDIES OF PHOSPHORYLASE ISOZYMES FROM THE RABBIT *
    • L. Schliselfeld
    • Biology, Medicine
    • Annals of the New York Academy of Sciences
    • 1973
    • 17