Kinetic studies of killer toxin K1 binding to yeast cells indicate two receptor populations
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
7979876
DOI
10.1007/bf00314477
Knihovny.cz E-resources
- MeSH
- Adsorption MeSH
- Cell Membrane metabolism MeSH
- Killer Factors, Yeast MeSH
- Kinetics MeSH
- Mycotoxins metabolism MeSH
- Receptors, Cell Surface classification metabolism MeSH
- Saccharomyces cerevisiae metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- K1 killer toxin MeSH Browser
- Killer Factors, Yeast MeSH
- Mycotoxins MeSH
- Receptors, Cell Surface MeSH
A recently described new method for determination of killer toxin activity was used for kinetic measurements of K1 toxin binding. The cells of the killer sensitive strain Saccharomyces cerevisiae S6 were shown to carry two classes of toxin binding sites differing widely in their half-saturation constants and maximum binding rates. The low-affinity and high-velocity binding component (KT1 = 2.6 x 10(9) L.U./ml, Vmax1 = 0.19 s-1) probably reflects diffusion-limited binding to cell wall receptors; the high-affinity and low-velocity component (KT2 = 3.2 x 10(7) L.U./ml, Vmax2 = 0.03 s-1) presumably indicates the binding of the toxin to plasma membrane receptors. Adsorption of most of the killer toxin K1 to the surface of sensitive cells occurred within 1 min and was virtually complete within 5 min. The amount of toxin that saturated practically all cell receptors was about 600 lethal units (L.U.) per cell of S. cerevisiae S6.
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