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Hæmagglutination of Erythrocytes coated with 6-Aminopenicillanic Acid

Nature volume 203, pages 412–413 (1964)Cite this article

Abstract

SINCE unaltered benzylpenicillin has not been shown to be capable of forming stable covalent bonds with proteins1, it has been suggested that the hapten complex associated with penicillin hypersensitivity involves the intermediate degradation compound D-benzylpenicillenic acid2–4. Levine and Ovary4 have shown that D-benzylpenicillenic acid will react with serum proteins, especially lysine ε-amino groups, to form the mixture of dia-stereomers of ε-N-(D-α-benzylpenicilloyl)-lysine groups. Such compounds are stable antigens giving wheal and erythema reactions in sensitized individuals. De Week and Eisen2, on the other hand, have produced evidence that D-benzylpenicillenic acid enters into mixed disulphide linkages especially with proteins enriched with SH groups and that antibody to such complexes has an affinity for the oxazolone ring structure of D-benzylpenicillenic acid.

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References

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Authors and Affiliations

  1. Department of Pathology, University of Natal, Durban, South Africa

    K. C. WATSON

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  1. K. C. WATSON
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WATSON, K. Hæmagglutination of Erythrocytes coated with 6-Aminopenicillanic Acid. Nature 203, 412–413 (1964). https://doi.org/10.1038/203412a0

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