Purified Protoplasmic Peptides of Mycobacteria: Chemical Composition of a Tuberculin-Active Glycopeptide
AUTOR(ES)
Stottmeier, K. D.
RESUMO
A tuberculin-active glycopeptide containing eight different amino acids and glucose was isolated from the protoplasm of Mycobacterium tuberculosis. A molecular weight of 4,000 to 5,000 was established by Sephadex gel filtration; other analyses showed a peptide to carbohydrate ratio of 9:1. These observations suggest a tentative composition of 3 to 4 residues of glucose, 12 residues each of aspartic and glutamic acids, 3 residues each of lysine, glycine, and serine, and 1 residue each of arginine, threonine, and alanine.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=248338Documentos Relacionados
- Synthesis and biological assays of peptides from a tuberculin-active protein.
- Purified Protoplasmic Peptides of Mycobacteria: Isolation of Species-Specific Peptides from Protoplasm of Mycobacteria
- Synthesis and biological assays of a peptide from a tuberculin-active protein.
- Purified Protoplasmic Peptides of Mycobacteria: In Vivo and In Vitro Comparison of the Species Specificity of Purified Protoplasmic Peptides and Purified Protein Derivatives of Mycobacterial Culture Filtrates
- Isolation, characterization, and biological properties of a tuberculin-active peptidoglycan isolated from the culture filtrate of Mycobacterium tuberculosis.