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Differential centrifugation of a sucrose homogenate of tuberculous mouse spleens was conducted to obtain sediments of cytoplasmic granules at 1,000 g, 3,900 g, 8,400 g, 15,000 g, and 25,000 g for 20 min. Acid phosphatase activity of the Triton-extract of each sediment indicated that the 15,000 g and 25,000 g sediments were rich in lysosomes. A large-molecular mycobactericidal fraction associated with cathepsin and acid phosphatase activities could be separated from the detergent-extracts of the 8,400 g, 15,000 g and 25,000 g sediments by gel-filtration on Sephadex G-150 column, but not from the 3,900 g sediment. From the lungs of the same group of mice, such a mycobactericidal fraction was not obtained. The active fraction from the spleens was further treated with one of the following three agents; 90% acetone, ethyl ether, and 2M urea. The mycobactericidal activity was found in the 90% acetone-soluble fraction and also in the small-molecular protein fraction released by ether-or urea-treatment. Both subfractions were free from the enzymatic activities. Their mycobactericidal activity was heat-stable at 100 C for 5 min. The difference between the two was that the 90% acetone-soluble subf raction was more effective with less Folin value and with less exposure time to the bacilli, but more dependent on acidic environment than the protein fraction.

SEPARATION AND PROPERTIES OF THE MYCOBACTERICIDAL PRINCIPLE FROM LYSOSOMAL COMPONENTS OF TUBERCULOUS MICE