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-3-水解酵素含有複合体より尿素による抗菌因子の分離,ことに正常動物との比較

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The lysosorne-rich fraction was separated from normal and BCG-revaccinated guinea pig lungs and was extracted with O.1 % Triton X-100. The extracts were fractionated by g elfiltration on Sepharose 2B column using 0.05M acetate buffer of pH 5.6 (Fig.1). The first protein peak associated with acid phosphatase and cathepsin activities from BCG-anim als (Fraction A) was found to be mycobactericidal, but the corresponding fraction f rom normal animals was not. These fractions were then treated with 2M urea and the extracts were fractionated by gel-filtration on Sephadex G-150 column (Fig.2). Fraction A from BCG anim als was divided into 2 protein peaks a and b by urea-treatment, the latter being separated from acid phosphatase activity. This small-molecular protein fraction was not obtained from no rmal animals.<BR>Table 1 demonstrates the summarized data of the mycobactericidal effects of those subfractions on H<SUB>87</SUB>Rv tubercle bacilli suspended in 0.05M acetate buffer of pH 5.6. The bacilli of 0.1mg per ml were exposed to each sample of indicated protein concentrations. The urea-released Fraction b was found to be active in killing tubercle bacilli, but it required more amount of protein and longer exposure time to express its mycobactericidal activity than Fraction A and Fraction a. In the environment of pH 7.4, the activity of each fraction was reduced. Fraction b was, however, more active than Fraction a at this pH (Table 2). A curious observation was that, though Fraction A of normal animals was not mycobactericidal, its 90% acetonesoluble moiety was highly active in this respect just as the corresponding sample from BCGanimals of our previous report. It might be possible to suggest that the 90% acetone-soluble substance is a "created" mycobactericidal fraction.<BR>When Fraction A of the normal animals was added to the corresponding fraction of the BCG-animals, the activity of the latter was reduced, which indicates a possible competition between the two fractions with respect to the contact with the bacilli. Fraction b appeared to be a small-molecular protein and it was heat-stable at 100°C and pH 5.6. However, lysozyme of the similar properties was not mycobactericidal in the same experimental conditions and in a much higher concentration (Table 4).
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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-3-水解酵素含有複合体より尿素による抗菌因子の分離,ことに正常動物との比較

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