Analysis of Aspergillus fumigatus catalases possessing antigenic activity.
Analysis of Aspergillus fumigatus water soluble fractions by electrophoresis on non-denaturing polyacrylamide gels (PAGE) showed the presence of at least three catalase bands. They were designated F, S1 and S2 in order of descending electrophoretic mobility with respect to the anode. The multiple enzyme forms appear to be distinct in their physicochemical properties. Enzyme bands S1 and S2 were simple catalases; the F band had an additional peroxidase function. All of the components were antigenic and differed in their binding to specific antibodies raised in rabbits with separate fractions of A. fumigatus mycelium. When serum from patients with aspergilloma, allergic bronchopulmonary aspergillosis, cystic fibrosis and chronic asthma were pre-incubated with A. fumigatus antigens and analysed by PAGE, 17 of 26 samples either abolished or reduced catalase activity. Enzyme F was a non-Concanavalin A (ConA)-binding antigen; the S1 and S2 enzymes were ConA-binding glycoprotein antigens. The major catalase band present in A. niger preparations represented only a minor component in A. fumigatus.
Hearn
V M
VM
Mycological Reference Laboratory, Central Public Health Laboratory, London.
Wilson
E V
EV
Mackenzie
D W
DW
D000818:Animals; D000908:Antibodies, Fungal / Q000097:blood*; D000946:Antigens, Fungal / Q000276:immunology*; D001228:Aspergillosis / Q000175:diagnosis* / Q000276:immunology; D001232:Aspergillus fumigatus / Q000201:enzymology* / Q000276:immunology; D002374:Catalase / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007118:Immunoassay; D012680:Sensitivity and Specificity
D000908:Antibodies, Fungal; D000946:Antigens, Fungal; D002374:Catalase