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- W2029022815 abstract "The rate of binding of Asp-hemolysin to human erythrocyte ghosts was determined by the single radial immunodiffusion technique. This binding rate was found to be reduced by various chemical reagents, yielding inhibition rates in the order of: glyoxal>TNBS>4-PDS>DTNB>HgCl2. These findings suggest that sulfhydryl and arginine-guanidino group(s) in the toxin may play an important role as a site of binding to the erythrocyte membrane. On the other hand, the hemolytic activity of Asp-hemolysin for chicken erythrocytes was significantly inhibited by arginine, lysine, and ornithine, while it was not affected by the similar compounds citruline, betaine, and histidine. Arginine was shown to be the most effective competitive inhibitor.On the basis of these results, the presence of a binding site in the Asp-hemolysin molecule is suggested. Furthermore, we suggest that the inhibition caused by arginine and related compounds is competitive." @default.
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- W2029022815 date "1985-01-01" @default.
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- W2029022815 title "Studies on toxin of aspergillus fumigatus XXI. Site of binding of asp-hemolysin to erythrocytes and mechanism of inhibition of hemolysis." @default.
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- W2029022815 doi "https://doi.org/10.3314/jjmm1960.26.70" @default.
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