Abstract
In the course of research on penicillin allergy (1, 11, 12), it was found that natural penicillin and its chemical parent nucleus, 6-aminopenicillanic acid (6-APA) contained traces of a macromolecular proteinaceous residue with striking allergenic properties in human subjects. Efforts were then made in the laboratory to remove these residues, but were only partly successful, because of the formation by penicillin in solution of a second residue with the characteristics of a polymer (1, 12, 13, 15). This finding, since confirmed by other workers (5, 17) led to the examination of a range of penicillins, of the related β-lactam antibiotics cephalosporins and of bacitracin, which is also a cyclic oligopeptide antibiotic. Spontaneous polymerization occurred in all the antibiotics examined (16).
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© 1970 Plenum Press, New York
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Stewart, G.T., Butcher, B.T., Wagle, S.S., Stanfield, M.K. (1970). Biopolymerization of Peptide Antibiotics. In: Johnson, J.F., Porter, R.S. (eds) Liquid Crystals and Ordered Fluids. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8214-0_3
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DOI: https://doi.org/10.1007/978-1-4684-8214-0_3
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