Synthesis and biological assays of a peptide from a tuberculin-active protein

The heptapeptide Asn-Gly-Ser-Gln-Met-Arg-Leu, part of a tuberculin-active intracellular mycobacterial protein and described in the literature as having residual tuberculin activity, has been synthesized. Biological assays of the synthetic peptide showed it to be recognized as an antigen of mycobacterial origin by its ability to elicit an early allergic reaction in Mycobacterium bovis BCG-infected mice. The synthetic peptide was shown to be devoid of any tuberculin activity in BCG-infected mice and in skin tests on Mycobacterium tuberculosis-sensitized guinea pigs. Purified protein derivative, complex mixture of proteins of unknown composition which is excreted into the culture medium by M. tuberculosis and is in wide use as a tuberculin-active preparation, was shown to weakly cross-react in radioimmunoassays with the synthetic heptapeptide when 125I-labeled heptapeptide and an anti-heptapeptide antiserum were used.

[1]  S. Kuwabara Purification and properties of tuberculin-active protein from Mycobacterium tuberculosis. , 1975, The Journal of biological chemistry.

[2]  E. Lederer,et al.  Minimal structural requirements for adjuvant activity of bacterial peptidoglycan derivatives. , 1974, Biochemical and biophysical research communications.

[3]  J. Meienhofer,et al.  Removal of the N alpha-benzyloxycarbonyl group from cysteine-containing peptides by catalytic hydrogenolysis in liquid ammonia, exemplified by a synthesis of oxytocin. , 1974, Journal of the American Chemical Society.

[4]  W. Hunter,et al.  The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. , 1973, The Biochemical journal.

[5]  W. Bauer,et al.  Boron tris(trifluoroacetate) for removal of protecting groups in peptide chemistry. , 1973, Angewandte Chemie.

[6]  L. Gráf,et al.  Revised amide location for porcine and human adrenocorticotropic hormone. , 1971, Acta biochimica et biophysica; Academiae Scientiarum Hungaricae.

[7]  C. Hirs [35] Detection of peptides by chemical methods , 1967 .

[8]  R. E. OFFORD,et al.  Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups , 1966, Nature.

[9]  Y. Shimonishi,et al.  A new method for releasing oxytocin from fully-protected nona-peptides using anhydrous hydrogen fluoride. , 1965, Bulletin of the Chemical Society of Japan.

[10]  S. Sakakibara,et al.  The N, O peptidyl shift in anhydrous hydrogen fluoride. , 1962, Biochemical and biophysical research communications.