[Comparison of the resistance during proteolysis of the antigenic structure of bovine serum albumin, chicken ovalbumin and their carbohydrate-modified forms].
A study was made of the effect of Maillard reaction between epsilon-amino groups of proteins and sugar carbonyl groups on the resistance of protein antigens (AG) to proteolysis in model systems and in the course of digestion and absorption in the gastrointestinal tract of adult rats. It was found that in vitro pepsin and trypsin inactivate antigenic determinants of bovine serum albumin (BSA) modified by carbohydrate less readily than those of basic protein. At the same time in the course of studying the cleavage and absorption of 3H-proteins and their glucose derivatives in the rat body, lack of a significant stabilization of modified BSA and ovalbumin as compared with non-modified ones was discovered. The discrepancy of the data derived in vitro and in vivo is likely to be related to the inadequacy of the available enzymatic models with regard to real conditions of digestion in the gastrointestinal tract.
D000818:Animals; D000941:Antigens / Q000032:analysis*; D002417:Cattle; D002645:Chickens; D004063:Digestion; D000939:Epitopes / Q000032:analysis; D005947:Glucose / Q000276:immunology* / Q000378:metabolism; D007114:Immunization; D066298:In Vitro Techniques; D007408:Intestinal Absorption; D010047:Ovalbumin / Q000276:immunology* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D012710:Serum Albumin, Bovine / Q000276:immunology* / Q000378:metabolism
D000941:Antigens; D000939:Epitopes; D012710:Serum Albumin, Bovine; D010047:Ovalbumin; D010447:Peptide Hydrolases; D005947:Glucose
Sravnenie ustoichivosti pri proteolize antigennoĭ struktury bych'ego syvorotochnogo al'bumina, kurinogo oval'bumina i ikh mofifitsirovannykh uglevodom form.