[Changes in the immunochemical properties of beta-lactoglobulin during proteolysis and exposure to various physico-chemical factors].
Heating of cow milk beta-lactoglobulin at 96 degrees, pH 8.0 led to the protein aggregation because of intermolecular disulfide exchange as shown by agarose gel immunoelectrophoresis, where additional precipitation strips were detected. At the same time, there was not observed dissociation of beta-lactoglobulin into separate fractions after proteolysis or denaturation in 8 M urea. beta-Lactoglobulin, its thermoaggregated and S-carboxymethyl denaturated forms exhibited similar anaphylactic effect on sensitized guinea pigs. Allergenic properties of beta-lactoglobulin appears to be unaltered in food hydrolyzates after thermal treatment and limited proteolysis.
Gmoshinskiĭ
I V
IV
Krzhechkovskaia
V V
VV
Zorin
S N
SN
D000818:Animals; D000941:Antigens / Q000737:chemistry* / Q000276:immunology; D002417:Cattle; D002853:Chromatography, Liquid; D006168:Guinea Pigs; D006868:Hydrolysis; D007114:Immunization; D007123:Immunoelectrophoresis, Two-Dimensional; D007782:Lactoglobulins / Q000737:chemistry* / Q000276:immunology; D008892:Milk / Q000737:chemistry / Q000276:immunology; D016269:Milk Hypersensitivity / Q000517:prevention & control*; D011489:Protein Denaturation
D000941:Antigens; D007782:Lactoglobulins
Izmenenie immunokhimicheskikh svoĭstv beta-laktoglobulina pri proteolize i nekotorykh fiziko-khimicheskikh vozdeĭstviiakh.