Amino acid sequence of tuberculin-active protein from Mycobacterium tuberculosis

Abstract

The complete amino acid sequence of tuberculin-active protein from tubercle bacilli was determined. The sequences of residues of tryptic, chymotryptic, and peptic peptides were established by Edman degradation and dansylation (5-dimethylaminonaphthalene-1-sulfonyl) and by digestion with carboxypeptidases A and B. Certain peptides were further degraded using partial acid hydrolysis. The aspartyl and glutamyl residues at positions 70 and 73 are present as amides. There is one intrachain disulfide bridge linking residues 27 and 59; there are no free sulfhydryls.