The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Improved Method for the Isolation and Properties of Tuberculin Active Peptides
YOSHIMI OKADASEIJI MORISAWAKENJI SYOJIMAMASAYASU KITAGAWASHOICHI NAKASHIMAYUICHI YAMAMURA
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1963 Volume 54 Issue 6 Pages 484-490

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Abstract

Tuberculin active peptide (TAP) was obtained from the bodies of tubercle bacilli, Aoyama B, in a high yield. One fourth μg. of TAP was as potent as 0.1ml. of standard 2, 000-fold diluted Old Tuberculin. TAP was fairly stable to the storage at room temperature at least for a year. Tuberculin activity of TAP was destroyed rapidly by the digestion with pro-teinase.
By the ultracentrifugal analysis and the measurement of optical rotatory dispersion, it was suggested that the molecular weight of TAP is rather small and TAP is characteristic of denatured protein.
TAP was proved to consist of several ac-tive principles by DEAE- and CM-cellulose column chromatography.

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© The Japanese Biochemical Society
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