1. A strain of Clostridium tertium was isolated from the soil which produced an enzyme acting on O(H) substance and group O red cells. The enzyme abolished not only their O(H) activity but also cross-reactivity with anti-pneumococci Type XIV chicken serum. The enzyme preparation decomposed O(H) substance, converting it into a substance which contained D-galactosamine and (or) D-glucosamine as antigenic determinant. This enzyme preparation also decomposed Lea substance. In addition to this enzyme, the strain produced A-decomposing enzyme.
2. These enzymes were found in a fraction which precipitated at 40-50% ammonium sulfate saturation of culture filtrate of the strain. By means of DEAE cellulose column chromatography, the enzyme decomposing O(H) and Lea could be separated from the A-decomposing enzyme. For both of them, the optimal pH ranged 6.3-7.2, and the optimal temperature 30°-37°C.
3. The actions of these enzymes were inhibited by such metal salts as mercuric chloride and copper sulfate. The enzymic action to decompose O(H) substance reacting with anti-O(H) antibody in eel serum was inhibited strongly by L-fucose, and slightly by lactose and D-galactose. The enzymic action to decompose O(H) substance reacting with anti-O(H) antibody in anti-Sh. dysenteriae chicken serum was inhibited strongly by lactose, D-galactose, and other sugars containing galactose, and weakly by L-fucose. And the enzymic action to decompose O(H) substance reacting with antibody in anti-pneumococci Type XIV chicken serum was inhibited by lactose, D-galactose, and N-acetyl-D-glucosamine. The Lea-decomposing action was inhibited strongly by L-fucose and D-galactose, and weakly by N-acetyl-D-glucosamine and N-acetyl-D-galactosamine. And the action of the A-decomposing enzyme was inhibited most strongly by N-acetyl-D-galactosamine, and also by lactose, D-galactose, and N-acetyl-D-glucosamine.

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The mononuclear phagocytes obtained from a normal mouse acquired cellular immunity against the infection with S. enteritidis in tissue cultures if the cells were treated with live vaccine of the same organism, whereas the cells treated with dead vaccine of S. enteritidis did not.

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1) The activity of heme α-methenyl oxygenase in the liver homogenate was found to be distributed in the supernatant Table V. The effect of dialysis and of boiled liver extract on the Activity of activated and not activated supernatant Table VI. Effects of preincubation time and of diet on the activity Of the supernatant fraction fraction by Schneider's method of differential centrifugation.
2) The enzyme activity in the supernatant fraction increases upon preincubation with the nuclear fraction.
3) The activator released from the nuclear fraction seems to be a low molecular substance.

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