CHEMICAL MODIFICATION OF TUBERCULIN PROTEIN:I. DINITROPHENYLATION AND PHENYLAZOBENZOYLATION

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  • OKADA YOSHIMI
    Department of Biochemistry, Faculty of Science, Osaka University

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Description

1. Tuberculin-active protein, hC, was dinitrophenylated with DNFB, but the tuberculin activity was not affected even after half of the lysine residues and all of the tyrosine residues were blocked by this reagent.<br> 2. When PABC was reacted with hC, 27 PAB-residues was introduced into 105g. of protein. Tuberculin activity remained unchanged after this treatment.<br> 3. No N-terminal amino acid was found in hC by means of the DNP-method.<br> The anther wishes to thank Prof. S. Akabori, Osaka University, for his continuous interest and advice during the course of this investigation, and to thank Prof. Y. Yamamura, Kyushu University, for his encouragement and guidance. The author also wishes to thank Dr. K. Ogura, Toneyama National Sanatorium, for his helpful advice, especially on the skin test technique.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 48 (1), 63-70, 1960

    The Japanese Biochemical Society

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