Abstract
An improved preparation of the sex-specific agglutinin from Hansenula wingei mating type 5 has been made by digesting the cell walls with subtilisin. It is similar to the previously reported agglutinin derived by digestion with snail enzymes in its specificity of agglutinating H. wingei mating type 21 only, and in sensitivity of its agglutinating activity to mercaptoethanol. It has less protein, 4%, a small sedimentation rate, 13.1 Svedbergs at 25 °, and a much smaller molecular weight, 570,000, and is more homogeneous in size than the previous preparation. After purification on phosphocellulose, it was shown to be pure in the sense that more than 85% was absorbed by H. wingei type 21 cells.
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