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IgE antibody-mediated shock reaction caused by topical application of chlorhexidine (1986)

OHTOSHI, T. ; YAMAUCHI, N. ; TADOKORO, K. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Clinical & experimental allergy 16 (1986), S. 0

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ISSN: 1365-2222

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: A case of an anaphylactic shock following topical application of chlorhexidine preparation is reported. Specific skin-sensitizing antibodies against chlorhexidine were demonstrated in the serum from the patient by a passive transfer test. IgE antibodies against chlorhexidine were also detected by radioallergosorbent technique (RAST). Paper discs conjugated with chlorhexidine-HSA (human serum albumin) significantly bound the IgE antibodies. Furthermore, all of the sera from seven other patients with shock reactions following the topical application of chlorhexidine preparation also showed high RAST counts. Both chlorhexidine gluconate and chlorguanide which represents approximately half a molecule of chlorhexidine inhibited the reaction in a dose-dependent fashion. It is suggested that the shock reactions following topical application of chlorhexidine are mediated by IgE antibodies against chlorhexidine and that chlorhexidine and chlorguanide share the same antigenic determinant.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2222.1986.tb00759.x

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Homology of L-gulonolactone oxidase of species belonging to Mammalia, Aves, and Amphibia (1981)

Nishikimi, M. ; Yamauchi, N. ; Kiuchi, K. ; [et al.]

Springer

Cellular and molecular life sciences 37 (1981), S. 479-480

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ISSN: 1420-9071

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Summary Immunological cross-reactivity of L-gulonolactone oxidase of different species (rat, chicken, and bullfrog) was tested by the Ouchterlony technique. Antiserum directed against the enzyme from chicken kidney reacted with rat liver enzyme as well as with bullfrog kidney enzyme. This finding suggests that there is, at least partly, sequence homology among the enzymes from species belonging to the three classes, Mammalia, Aves, and Amphibia.