Premium
Enzyme‐linked immunosorbent assay for detection of antibodies to the unmodified beta‐lactam ring
Author(s) -
Klein G. F.,
Stanzl U.,
Fritsch P. O.,
Varga J. M.
Publication year - 1993
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/j.1398-9995.1993.tb00705.x
Subject(s) - penicillin , antibody , chemistry , carbodiimide , immunoglobulin e , monoclonal antibody , enzyme , lactam , covalent bond , microbiology and biotechnology , biochemistry , antibiotics , immunology , stereochemistry , medicine , biology , organic chemistry
Dose‐ and pH‐ dependent carbodiimide‐mediated coupling of Penicillin‐G to polystyrene microtiter‐plates that leaves the beta‐lactam ring unchanged is described. A new ELISA method was developed using Penicillin‐G coated plates. The binding of 3 different monoclonal antibodies as well as human IgG antibodies of the IgG 1 and IgG 3 subclasses is demonstrated, whereas IgG 2 , IgG 4 and IgE antibodies did not bind. Thus, covalently coupled Penicillin‐G can be used to study the immune‐response to the unchanged β‐lactam ring in patients receiving penicillin therapy. The new method is complementary to hitherto described techniques, which generally only allow detection of antibodies binding to penicilloyl‐groups.