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Studies on toxin of aspergillus fumigatus 22. fashion of binding of aspartyl hemolysin to human erythrocytes and aspartyl hemolysin binding proteins of erythrocyte membranes


Studies on toxin of aspergillus fumigatus 22. fashion of binding of aspartyl hemolysin to human erythrocytes and aspartyl hemolysin binding proteins of erythrocyte membranes



Microbiology and Immunology 29(2): 91-102



ISSN/ISBN: 0385-5600

The fashion of binding of Asp-hemolysin to human erythrocytes and the isolation of Asp-hemolysin-binding proteins from erythrocyte membranes were investigated by the immunocytochemical technique and affinity chromatography. Asp-hemolysin bound best at a pH range from 5 to 7. The erythrocytes treated with Asp-hemolysin showed diffuse, ring-like or cap-like staining by the peroxidase-labeled antibody method under the light microscope. The distribution of Asp-hemolysin on the erythrocyte surface was clearly observed as patches or caps in the scanning electron microscope. The erythrocyte ghosts were extracted with 1% sodium deoxycholate-0.1 M Tris-HCl buffer (pH 7.5) containg 0.2 M NaCl and 1 mM EDTA, and the extract was chromatographed on an affinity column consisting of Asp-hemolysin attached to activated thiol-Sepharose B. Four proteins present in the membrane extract were retained by activated thiol-Sepharose 4B and eluted with 50 mM cysteine as toxin-membrane components. Sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that the polypeptides correspond to band 2.1, 1 protein of the 2 region, band 3 and band 7 in the Steck nomenclature system.

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Accession: 006523251

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Related references

Studies on toxin of Aspergillus fumigatus. XXII. Fashion of binding of Asp-hemolysin to human erythrocytes and Asp-hemolysin-binding proteins of erythrocyte membranes. Microbiology and Immunology 29(2): 91-101, 1985

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