The purification and characterisation of cervine IgM and IgG.
A procedure is described for the isolation of immunoglobulin G (IgG) and immunoglobulin M (IgM) from hyperimmune cervine serum. Hybrids of red deer (Cervus elaphus) and wapiti (Cervus canadensis) were immunised with keyhole limpet hemocyanin (KLH). An immunoglobulin-containing fraction was precipitated from the hyperimmune serum using ammonium sulphate. The antigen-specific immunoglobulins were purified by KLH-conjugated sepharose affinity chromatography and further separated into IgM and IgG by gel-filtration chromatography. Purified immunoglobulin was analysed by polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weights and isoelectric points of the composite chains of cervine IgG and IgM are presented.
Hibma
M H
MH
Microbiology Dept., University of Otago, Dunedin, New Zealand.
Griffin
J F
JF
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003670:Deer / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006433:Hemocyanins / Q000008:administration & dosage / Q000276:immunology; D007114:Immunization; D007074:Immunoglobulin G / Q000276:immunology / Q000302:isolation & purification*; D007075:Immunoglobulin M / Q000276:immunology / Q000302:isolation & purification*; D007526:Isoelectric Point; D008297:Male
D007074:Immunoglobulin G; D007075:Immunoglobulin M; D006433:Hemocyanins; C032808:keyhole-limpet hemocyanin