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Interaction of snake venom cardiotoxin (a membrane-disruptive polypeptide) with human erythrocytes

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Abstract

The action of 7.2 µM cardiotoxin on 0.25% human erythrocytes in a plasma extender solution was studied by the interaction of toxin with intact red blood cells and subsequent hemolysis of the cells. The binding of toxin to cells was completed within 10 min, whereas the membrane rigidity was weakened in a non-lytic period for about 25 min. The toxin molecules bound almost exclusively to the membrane. The bound toxin could not be liberated with either 0.5% Triton X-100 or 0.1 N NaOH. The degree of binding was slightly reduced in the presence of 10 mM mono- and divalent inorganic salts. The action of toxin might weaken the in situ association of several proteins that are linked with band 3 protein of the membrane, thus making the cells fragile and altering the shape of the cell to a smooth sphere.

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Authors and Affiliations

  1. Institute of Biochemical Sciences, National Taiwan University, 107, Taipei, Taiwan, China

    Yee-Hsiung Chen, ChienTsung Hu & Chung-Ching Juan

  2. Institute of Biological Chemistry, Academia Sinica, 107, Taipei, Taiwan, China

    Yee-Hsiung Chen & Ruey-Fen Liou

  3. Cardiovascular Research Institute, University of California, 94143, San Francisco, CA, USA

    Jen Tsi Yang

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  1. Yee-Hsiung Chen
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  2. Ruey-Fen Liou
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  3. ChienTsung Hu
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  4. Chung-Ching Juan
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  5. Jen Tsi Yang
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Chen, YH., Liou, RF., Hu, C. et al. Interaction of snake venom cardiotoxin (a membrane-disruptive polypeptide) with human erythrocytes. Mol Cell Biochem 73, 69–76 (1987). https://doi.org/10.1007/BF00229378

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  • DOI: https://doi.org/10.1007/BF00229378

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