Abstract

When cells of Chondrococcus coralloides were grown on different bacteria and yeast as the only substrates, a pronounced lysis zone in the agar was observed after 3 days of incubation. Gelatine was liquified by the growing organism after 12 h. Enzyme preparations from the culture medium of Chondrococcus lysed only cells from Micrococcus lysodeikticus, at reasonable rates, and they were very active against casein and N-α-benzoyl-l-arginine-ethylester · HCl. The lytic activity in the culture medium decreased rapidly after the culture reached the stationary growth phase. A fifty-fold purification of the bacteriolytic activity was achieved by step-wise acetone precipitation. Chromatography of this preparation on Sephadex G-100 revealed the presence of four fractions, one proteolytic, two bacteriolytic and one fraction with both bacteriolytic and proteolytic activity. The bacteriolytic activity had a pH-optimum of pH 8, a stability optimum at pH 8 and was more stable in the alkaline region than in the acid. EDTA and Mg++ inhibited the lysis. The proteolytic activity against N-α-benzoyl-l-arginine-ethylester · HCL had a pH-optimum of pH 7. The Kmof this reaction was 6.5×10-4.

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