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  • serpin
  • studies of serpin structure and function (the fact that ovalbumin does not inhibit proteases means that by comparing its structure with that of inhibitory serpins, the structural characteristics required for inhibition can be determined). (wikipedia.org)
  • When heated, ovalbumin undergoes a conformational change from its soluble, serpin structure into an insoluble all-β-sheet structure with exposed hydrophobic regions. (wikipedia.org)
  • Secondary structure of OVAX is similar to that of ovalbumin, but the three-dimensional model of OVAX reveals the presence of a cluster of exposed positive charges, which potentially explains the affinity of this ov-serpin for heparin, as opposed to ovalbumin. (sigmaaldrich.com)
  • sequence
  • Altogether, these results suggest that OVAX and ovalbumin, although highly similar in sequence, have peculiar sequential and/or structural features that are likely to impact their respective biological functions. (sigmaaldrich.com)
  • native
  • From measurements of the displacement of the precipitin curve of irradiated ovalbumins from the position of the curve for native ovalbumin the loss of activity due to primary ionizations was determined. (jimmunol.org)
  • Solutions of the γ-irradiated ovalbumins were fractionated by promptly precipitating the radiation-denatured molecules at the isoelectric point of native ovalbumin, and by heating the neutral systems at 50°, 60° and 68°C and by precipitating the thermolabile constituents at the isoelectric point. (jimmunol.org)
  • model
  • The aim of this work was to evaluate the properties of poly-epsilon-caprolactone (PCL) microparticles as adjuvants in immunotherapy using ovalbumin (OVA) as an allergen model. (cun.es)
  • high
  • Samples of lyophilized ovalbumin were irradiated, under vacuum in a high energy, uniform field of γ-rays, to absorb dosages of 30, 60 and 100 electron volts/molecule (6.5, 13.0 and 21.7 × 10 6 rads). (jimmunol.org)
  • signal
  • The functional signal for membrane translocation of ovalbumin becomes accessible when the nascent chain is 50 to 60 residues long. (abcam.com)