La détoxication des toxines protéiques par le formol: mécanismes supposés et nouveaux développements

Summary The possible mechanisms involved in the detoxification of proteic toxins by formaldehyde are discussed. Using diphtheria or tetanus toxoids as model compounds, the appearance of acid-resistant derivatives in the acid hydrolyzates of these toxoids was established. One of the derivatives was shown to be a Mannich-like compound linking the e-amino group of a lysyl residue by a methylenic bridge to a tyrosyl residue in position 3 of the phenol ring. This structure was confirmed by synthesis. Two further derivatives were tentatively identified as being formed by the linkage of two lysyl residues to a tyrosyl residue or of two lysyl residues to one another by a methylenic bond. In addition, it is reported that tyrosyl as well as histidyl residues participate in toxicity, whereas lysyl residues do not. The latter fact led to postulate that lysyl residues interfere with the detoxification process by allowing methylenic bridges to be formed with amino-acid residues, in particular tyrosyl and/or histidyl residues, directly implied in toxicity.