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Immobilization of chicken liver fructose 1,6-bisphosphatase on CNBr-activated Sepharose

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Summary

Chicken liver fructose 1,6-bisphosphatase is readily immobilized on CNBr-activated Sepharose. The immobilization alters some enzymatic properties. They include broader pH activity curve, loss of activation by K+ or NH +4 , increased resistance to inactivation by trypsin, decreased sensitivity to AMP inhibition, and loss of cooperative interaction among AMP-binding sites. The immobilized enzyme retains about 38% or 19% of the specific activity of the native enzyme when the activity is measured in the absence or presence of K+, resepctively.

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Authors and Affiliations

  1. Department of Chemistry, Morehouse College, 30314, Atlanta, Georgia, USA

    G. Y. Han, Y. H. Wang, H. C. McBay, J. Johnson & P. F. Han

  2. Science Research Institute, Atlanta University Center, 30310, Atlanta, Georgia, USA

    G. Y. Han, Y. H. Wang, H. C. McBay, J. Johnson & P. F. Han

Authors
  1. G. Y. Han
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  2. Y. H. Wang
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  3. H. C. McBay
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  4. J. Johnson
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  5. P. F. Han
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Additional information

This work was supported by grant RR-8006 from the General Research Branch, Division of Research Resources, NIH (USA).

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Han, G.Y., Wang, Y.H., McBay, H.C. et al. Immobilization of chicken liver fructose 1,6-bisphosphatase on CNBr-activated Sepharose. Experientia 41, 1149–1151 (1985). https://doi.org/10.1007/BF01951702

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  • DOI: https://doi.org/10.1007/BF01951702

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