Studies on the antibody response of Lama glama--evaluation of the binding capacity of different IgG subtypes in ELISAs for clenbuterol and BSA

• Published in: Veterinary immunology and immunopathology Vol. 83; no. 1-2; pp. 1 - 9
• Main Authors: Lange, I G, Daxenberger, A, Meyer, H H
• Format: Journal Article
• Language: English
• Published: Netherlands 01.11.2001
• Subjects: Adrenergic beta-Agonists - immunology; Animals; Blotting, Western - veterinary; Camelids, New World - immunology; Chromatography, Affinity - veterinary; clenbuterol; Clenbuterol - immunology; Electrophoresis, Polyacrylamide Gel - veterinary; Enzyme-Linked Immunosorbent Assay - veterinary; Immunoglobulins - analysis; Immunoglobulins - biosynthesis; Lama glama; Male; protein A; protein G; Sensitivity and Specificity; Serum Albumin, Bovine - immunology; Staphylococcal Protein A - immunology
• ISSN: 0165-2427; 1873-2534
• DOI: 10.1016/S0165-2427(01)00376-2

Camelidae are known to produce three subtypes of immunoglobulin G (IgG), two of which are devoid of light chains. Two llamas (Lama glama) were immunised against clenbuterol-bovine serum albumin (BSA). Enzyme-linked immunosorbent assays (ELISAs) for clenbuterol and BSA on the basis of protein A-coated microtitration plates were established to investigate the titre development. Three subclasses of IgG (IgG(1): 29+66KDD, IgG(2): 52KDD, IgG(3): 56KDD) depending on their different binding properties to protein A and protein G could be separated chromatographically. Only IgG(1), which consists of conventional four-chain antibodies, bound to clenbuterol, whereas all forms of heavy-chain antibodies merely bound BSA.