VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Changes in the immunochemical properties of beta-lactoglobulin during proteolysis and exposure to various physico-chemical factors

   
Gmoshinskiĭ I.V., Krzhechkovskaia V.V., Zorin S.N.
PubMed Id: 2251783
Year: 1990  Volume: 36  Issue: 5  Pages: 11-15
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.
Download PDF:  
Citation:

Gmoshinskiĭ, I. V., Krzhechkovskaia, V. V., Zorin, S. N. (1990). Changes in the immunochemical properties of beta-lactoglobulin during proteolysis and exposure to various physico-chemical factors. Voprosy Meditsinskoi Khimii, 36(5), 11-15.
References
 2002 (vol 48)
 2001 (vol 47)
 2000 (vol 46)
 1999 (vol 45)
 1998 (vol 44)
 1997 (vol 43)
 1996 (vol 42)
 1995 (vol 41)
 1994 (vol 40)
 1993 (vol 39)
 1992 (vol 38)
 1991 (vol 37)
 1990 (vol 36)
 1989 (vol 35)
 1988 (vol 34)
 1987 (vol 33)
 1986 (vol 32)
 1985 (vol 31)
◄        ►