Biochemistry (Moscow)

, Volume 75, Issue 4, pp 437–442 | Cite as

Structural changes of a protein bound to a polyelectrolyte depend on the hydrophobicity and polymerization degree of the polyelectrolyte

  • S. V. Stogov
  • V. A. Izumrudov
  • V. I. MuronetzEmail author


Influence of polyelectrolytes of different chemical structure and degree of polymerization on aggregation and denaturation of the oligomeric enzyme glyceraldehyde-3-phosphate dehydrogenase has been studied to ascertain molecular characteristics of the polymer chains providing the efficient prevention of aggregation of the enzyme without drastic changes in its structure and catalytic activity. The best polymers meeting these requirements were found to be hydrophilic high-molecular-weight polyelectrolytes forming stable complexes with the enzyme. The revealed pronounced negative effect of short polymer chains on the enzyme must be taken into account in the design of protein-polyelectrolyte systems by using thoroughly fractionated polymer samples containing no admixture of charged oligomers.

Key words

glyceraldehyde-3-phosphate dehydrogenase polysulfoanions protein-polyelectrolyte complexes thermoaggregation suppression differential scanning calorimetry 



degree of polymerization


dextran sulfate


D-glyceraldehyde-3-phosphate dehydrogenase


polyacrylic acid


potassium poly-2-acrylamido-2-methyl-1-propane sulfonate


sodium polyanethol sulfonate


polymethacrylic acid


sodium polystyrene sulfonate


potassium polyvinyl sulfate


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Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  • S. V. Stogov
    • 1
  • V. A. Izumrudov
    • 2
  • V. I. Muronetz
    • 1
    • 3
    Email author
  1. 1.Faculty of Bioengineering and BioinformaticsLomonosov Moscow State UniversityMoscowRussia
  2. 2.Faculty of ChemistryLomonosov Moscow State UniversityMoscowRussia
  3. 3.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

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