Abstract
The major protein antigens of the yeast cell wall, TLA a and TLA b, were found to specifically bind with the alkali-soluble fraction (ASF) which was prepared from yeast cells (Saccharomyces cerevisiae) essentially by the method of Manners et al. Also, TLA a and TLA b were found to be present in the alkali-soluble fraction of yeast cells. This fraction was prepared from yeast cell homogenates after solubilizing by alkali (pH 9.0) followed by precipitating with acid (pH 6.0). The binding of TLA a and TLA b with ASF was completed rapidly. The optimum pH for the binding was 6.0. Concentrations of sodium chloride higher than 0.06 M and 0.1M inhibited the binding of TLA a and TLA b, respectively. TLA a or TLA b-ASF complexes were dissociated commpletely in 0.2M and 0.6M NaCl solution, respectively. ASF was reconstituted on the surface of protoplasts after 3 hr of incubation.
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