Isolation and characterisation of immunoglobulin g and IgG subclasses of the African elephant (Loxodonta africana).

Immunoglobulins were precipitated from pooled African elephant sera with ammonium sulphate and separated by gel filtration and fast protein liquid chromatography (ion exchange). Analysis of the fractions by SDS-PAGE showed IgG of 150 kDa with up to five subclasses, each having heavy chains of 57 kDa and light chains of 27 kDa. Three monoclonal antibodies against human IgG and polyclonal antibodies against canine, bovine, cameline, equine, phocine and feline IgG showed strong cross-reactivity with the African elephant IgG subclasses. No serum molecules corresponding to IgM or IgA could be detected, even when ammonium sulphate precipitation was used at 50% saturation.