BCG再接種モルモットの肺の細胞顆粒分画からの抗結核菌物質の分離とその性状-2-表面活性剤による抽出とゲル濾過法による分離

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A huge-molecular mycobactericidal fraction associated with cathepsin and acid phosphatase activities was separated from detergent-extract of the lung granular fraction of BCG-revaccinated guinea pigs by gel-filtration on Sepharose 2 B column (Fig.1, Fig.2, Table 1). The mycobactericidal activity was heat-stable at 100°C and pH 5.6 for 10 minutes, but the enzymatic activities were lost. Further fractionation was conducted using organic solvents (Fig.3, 4), and the mycobactericidal moiety was obtained as 90% acetone-soluble and ether-insoluble components of still high molecular weight. The components were free from the enzymatic activities. Separation of such mycobactericidal components was also successful from the extract prepared by freezing and thawing, but this fraction was negative in cathepsin activity unlike the preparation by the detergent.<BR>A discussion was m a de that the mycobactericidal principle might exist in the membrane structure associated with lysosomal hydrolases, but as a factor distinct from them.
一般社団法人日本結核病学会の論文