Independent thermal unfolding of ovomucoid domains

Effect of heat treatment on hen’s egg ovomucoid: An immunochemical and calorimetric study

“…It has to be pointed out that ovomucoid experiments an important refolding while cooling after heat treatment, as it has been observed in the DSC study of the present work and in previous studies (Matsuda, Watanabe, & Sato, 1981). The partial restoration of ovomucoid while the samples are cooling in the capillary tubes could have a strong contribution to the nonlinear behaviour shown by the process of loss of ovomucoid immunoreactivity.…”

“…Studies have shown that the thermal transitions of the different domains of ovomucoid, though independent, are all produced in a very short range of temperature at neutral pH (Matsuda et al, 1981). It is possible that at another pH there is a shift in the transition of the different domains of ovomucoid, which could explain that the peak observed at basic pH showed two maxima.…”

Recognition of Native and/or Thermally Induced Denatured Forms of the Major Food Allergen, Ovomucoid, by Human IgE and Mouse Monoclonal IgG Antibodies

“…Second, OM does not aggregate by heating and H-OM still expresses allergenicity. 16) The reversible conformational change of OM during heat treatment has been analyzed, 30,31) however, this does not mean that OM is native even after heating. As we have shown in this paper, the establishment of mAbs specific to N-or H-OM provides strong evidence for the presence of an irreversibly heat-denatured form of OM.…”

Intracellular Retention and Subsequent Release of Bovine Milk Lactoferrin Taken Up by Human Enterocyte-Like Cell Lines, Caco-2, C2BBe1 and HT-29

“…Goat anti-LF (IgG fraction) was from Brthyl Laboratories. The rabbit anti-OM IgG fraction was prepared from anti-OM serum 23) by ammonium sulfate precipitation followed by anionexchange chromatography in a column of DEAE-Sephacel (GE Healthcare Life Science). The mouse anti-human IntL monoclonal antibody (Saly-1) was obtained from Alexis Biochemicals.…”