Japanese Journal of Medical Science and Biology
Online ISSN : 1884-2828
Print ISSN : 0021-5112
ISSN-L : 0021-5112
AFFINITY OF LYSOSOMAL ACID PHOSPHATASE TO THE SURFACE OF THE TUBERCLE BACILLUS
金井 興美
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ジャーナル フリー

1967 年 20 巻 5 号 p. 401-411

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“Lysosomal” fraction was obtained from 0.25 M sucrose homogenate of mouse lungs and spleens by differential centrifugation. The contents of lysosomes were separated from the fraction as the supernatant of centrifugation at 15, 000 g for 20 min, after treatment with Triton X-100 in concentrations from 0.05 to 0.5%. Viable tubercle bacilli, when incubated with the contents at 37C, acquired the lysosomal type of acid phosphatase activity and lost (or masked) the same kind of enzyme activity peculiar to the bacilli. Additional investigations using cell walls of the bacilli and by a cytochemical approach indicated that lysosomal acid phosphatase was bound on the surface of the bacilli. This result is compatible with our previous finding that “in vivo grown tubercle bacilli” isolated mechanically from infected mouse lungs have the host-originated acid phosphatase on their surface, and also with the current state of knowledge concerning phagocytosis, particularly the degranulation phenomenon. As the initial step of tuberculous infection, attachment of the lysosomal contents to tubercle bacilli engulfed into phagocytes was suggested.
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