Purification of horse immunoglobulin isotypes based on differential elution properties of isotypes from protein A and protein G columns.
Elution properties of horse immunoglobulin isotypes from protein A and protein G columns were examined. IgGa and IgGb isotypes were bound to protein A and protein G columns and were eluted by adjusting the pH of the elution buffer from 8.0 to 2.0. IgGc bound to protein G column but not to protein A column while IgG(T) bound to both columns. IgM and IgA apparently appeared not to bind to either column. New methods for purification of serum isotypes were developed using protein A and protein G columns as well as formerly established methods. Using these methods, it was possible to obtain purified isotypes for establishment of immunological assays for practical clinical use.
Sugiura
T
T
Epizootic Research Station, Equine Research Institute, The Japan Racing Association, Shimotuga-gun, Tochigi, Japan.
Imagawa
H
H
Kondo
T
T
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006736:Horses; D007122:Immunoelectrophoresis; D007132:Immunoglobulin Isotypes / Q000302:isolation & purification*; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D013205:Staphylococcal Protein A / Q000737:chemistry*
C029152:G-substrate; D007132:Immunoglobulin Isotypes; D009419:Nerve Tissue Proteins; D013205:Staphylococcal Protein A