title: Isolation of horse IgG with protein A.
abstract: 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.
authors.affiliation: Centro de Pesquisa e Formação, Instituto Butantan, São Paulo, Brasil.
authors.forename: I
authors.initials: I
authors.lastname: Fernandes
authors.forename: H A
authors.initials: HA
authors.lastname: Takehara
authors.forename: I
authors.initials: I
authors.lastname: Mota
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D006736:Horses; D007074:Immunoglobulin G / Q000302:isolation & purification* / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000378:metabolism*
chemical_list: D007074:Immunoglobulin G; D013205:Staphylococcal Protein A