Abstract
A growth inhibitory factor of yeast cells produced by a strain of Basidiomycetes was purified by ion-exchange chromatography on CM-Sephadex and DEAE-Sephadex, and gelfiltration. The properties of the purified factor were studied with column chromatography, disc electrophoresis and analytical ultracentrifugation. N-Terminal of the factor was analyzed by the DNP-method. The results indicated that the active principle was a homogenous protein with s20, W value of 1.7×10-13, a molecular weight of approximately 17, 000, and no free N-terminal when examined by the DNP-method.
The purified principle exhibited inhibitory action against yeast growth and lysis against yeast glucan. These findings suggested that the active priciple is a β-glucanase.
