Adsorção de IgG humana em duas matrizes porosas derivatizadas com o ligante histidina

AUTOR(ES)
DATA DE PUBLICAÇÃO

2000

RESUMO

Affinity adsorption explores the characteristics that certain compounds have to selectively interact with substances or classes of substances. This technique has been used to purify proteins in small and large scale and also to remove autoantibodies from plasma of autoimmune patients. In an extracorporeal treatment, the autoantibodies are retained in a column that contains an affinity ligand immobilized in an insoluble matrix. The unretained fraction containing the plasma proteins different from the autoantibodies can be returned to the patient. In this work, the behavior of IgG adsorption either onto poly ethylene vinyl alcohol (pEV A) hollow-fiber membranes or onto metacrylate gels (Toyopearl) containing histidine as affinity ligand was studied. The IgG adsorption in both supports was feasable. The selectivity studies as well as the static and dynamic adsorption experiments showed that the IgG adsorption onto PEV A hollow-fibers was more efficient than onto Toyopearl, independently ifHepes pH 7.0 or Tris-HCI 7.4 buffer were used. The adsorption isotherms of IgG in the supports with or without ligand showed that there is also non-specific adsorption of the protein onto the matrix surface. The amount of specifically adsorbed protein was determined by the elution and regeneration of the support following extensive washing of the particles with buffer. The values of the adsorption capacity constant (Qm), dissociation constant of the IgG-histidine complex (Kd), adsorption constant (ka), and desorption constant (kd) indicated that both systems have approximately the same affinity for the IgG (10.5 M) and that PEV A hollow-fibers have a large specific adsorption capacity. This behavior was observed for temperatures of25 and 37°C

ASSUNTO(S)

doenças auto-imunes adsorção sangue - circulação extracorporea imunoglobulina g

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