Isolation of horse IgG with protein A.
Horse immunoglobulins were obtained from normal serum defatted with dextran sulfate and precipitated with ammonium sulfate. Eight mg of this preparation was submitted to affinity chromatography with protein A-Sepharose CL-4B. Low temperature (4 degrees C) and a starting buffer at pH 8.0 were conditions required for all IgG subclasses to bind to protein A, even those with low affinity. The IgGs bound to protein A were eluted with glycine buffer at pH 2.8. The yield was about 90%. It is suggested that isolated IgG, instead of whole Igs, be used in serum therapy, reducing the amount of Igs and diminishing serum-related reactions.
Fernandes
I
I
Centro de Pesquisa e Formação, Instituto Butantan, São Paulo, Brasil.
Takehara
H A
HA
Mota
I
I
D000818:Animals; D002846:Chromatography, Affinity; D006736:Horses; D007074:Immunoglobulin G / Q000302:isolation & purification* / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000378:metabolism*
D007074:Immunoglobulin G; D013205:Staphylococcal Protein A