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Journal of Solid Phase Biochemistry

, Volume 3, Issue 2, pp 107–117 | Cite as

Activation of prephenate dehydratase by adsorption to agarose derivatives

  • Patricia Campbell
  • George I. Glover
Article
  • 20 Downloads

Abstract

A series of potential affinity adsorbents for prephenate dehydratase were synthesized by coupling allosteric effectors to agarose with and without spacer arms. Only cationic ligands containing a hexamethylene spacer arm adsorbed the enzyme. Activity could be removed from aminohexyl- and glycyl-aminohexyl-agaroses with 0.5 M NaCl (with loss of activity), 0.4 M phosphate, or 140 mM hexanediamine, but was not removed from ala-aminohexyl-, phe-aminohexyl-, met-aminohexyl-, leu-aminohexyl-, or phenylpyruvyl-aminohexyl-agaroses or by Gly, Ala, Phe (inhibitor), Met or Leu (both activators). Urea (1.0 M), 1 mM phosphate, 50% glycerol in phosphate or prephenic acid (substrate) did not release enzymatic activity from any of the gels. The gel-bound enzyme was found to have enhanced activity comparable to that of the methionine-activated soluble enzyme. The site and mode of the enzyme immobilization are discussed in relation to the possible hydrophobic/ionic subunit-subunit interactions.

Keywords

Hydrophobic Amino Acid Standard Buffer Phenylpyruvate Aminohexyl Hexanediamine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc. 1979

Authors and Affiliations

  • Patricia Campbell
    • 1
  • George I. Glover
    • 1
  1. 1.Department of ChemistryTexas A&M UniversityTexas

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