Fragmentation of human albumin with proteolytic enzymes and its antigenicity with special reference to human-specificity.
Human albumin prepared by the trichloroacetic acid method was treated with bromelin, ficin, papain, pronase or trypsin. Pronase- or trypsin-treated albumin showed four fragments on polyacrylamide disc electrophoresis. When rabbit antiserum to pronase-treated albumin was adsorbed with monkey albumin, antibody with human specificity was completely abolished, whereas anti-albumin serum adsorbed with pronase-treated albumin retained the antibody to human albumin. It was considered that antigenic site with human specificity in albumin structure was inactivated by pronase.
D000941:Antigens; D001801:Blood Stains; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D010447:Peptide Hydrolases; D011402:Pronase; D012709:Serum Albumin / Q000276:immunology*; D013045:Species Specificity
D000941:Antigens; D012709:Serum Albumin; D010447:Peptide Hydrolases; D011402:Pronase