Abstract
The sex-specific agglutinin from mating type 5 of Hansenula wingei contained six disulfide bonds per particle. It could he inactivated by disulfide-cleaving agents and converted to a mixture of two components having sedimentation rates of approximately 2 and 13 S, compared with the original of s 25, w = 13.1. The 2S component made up 9% and the 13S, 81% of the total material. On dialysis in pH 7.6 buffer, the reduced products regained 25–77% of the original agglutinative activity. After separation of the two reduced components by gel filtration, tests disclosed that activity was regained gained only when both components were dialyzed together. Evidently, 5-agglutinin contains a sensitive, interchain disulfide bond system which unites several agglutinating elements in each particle with a large inert matrix.
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