DETAILED DESCRIPTION What is claimed is: 1.
A tuberculin active simple protein from Mycobacterium tuberculosis strain Aoyama B which is characterized by the following amino acid sequence: ##EQU3## wherein Asn and Gln represent asparagine residue and glutamine residue, respectively, and the remaining abbreviations represent the usual meanings and wherein the cysteine residues at positions 27 and 59 form one intra-chain disulfide bridge, said protein also being characterized by the following amino acid composition per molecule: Lys 4, His 1, Arg.
4, Cys 2, Asp 11 (containing one asparagine residue), Thr 5, Ser 4, Glu 11 (containing one glutamine residue), Pro 5, Gly 7, Ala 11, Val 8, Met 1, I1e 4, Leu 7, Tyr 2 and Phe 2.
2.
A tuberculin active fragment which is prepared by enzymatic digestion of the tuberculin active simple protein of claim 1 and which has the following tuberculin active group therein: -Asn-Gly-Ser-Gln-Met-.
3.
A tuberculin active pentapeptide whose amino acid sequence is as follows.
##EQU4##
Description:
The present invention is concerned with tuberculin active simple proteins and peptides which have the following peptide linkage.
--Asn--Gly--Ser--Gln--Met-- As a tuberculin active functional group.
It is well known that purified protein derivative(PPD) from extracellular old tuberculin(OT) has been used exclusively for the diagnosis of tuberculosis.
Unfortunately, in addition to tuberculin active proteins, PPD contains other inactive proteins, nucleic acids, polysaccharides and fatty acids.
As tuberculin active simple proteins have not been obtained, their physico-chemical, chemical and biological properties have not been determined.
The present inventors have succeeded in isolating tuberculin active simple proteins from the cells of tubercle bacilli and have obtained them as crystalline forms.
Subsequently the amino acid sequences and amino acid compositions per molecule of the obtained proteins have been determined.
Besides, they have obtained tuberculin active peptides by hydrolyzing the above obtained proteins and fractionating the resultant hydrolysates
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