Isolation of horse IgG with protein A
Braz. j. med. biol. res
;
24(11): 1129-31, 1991. ilus, tab
Artículo
en Inglés
| LILACS
| ID: lil-105492
RESUMO
Horse immunoglobulins were obtained from normal 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-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%. Its suggested that isolated IgG, instead of whole Igs, be used in serum therapy, reducing the amount of Igs and diminishing serum-related reactions
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Índice:
LILACS (Américas)
Asunto principal:
Proteína Estafilocócica A
/
Inmunoglobulina G
Límite:
Animales
Idioma:
Inglés
Revista:
Braz. j. med. biol. res
Asunto de la revista:
Biologia
/
Medicina
Año:
1991
Tipo del documento:
Artículo
/
Congreso y conferencia
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