Jy. Shi et Ra. Goffe, COMPREHENSIVE STUDY ON BINDING-CAPACITY OF HUMAN-IMMUNOGLOBULIN-G TO AVID-AL AFFINITY GEL, Journal of chromatography, 686(1), 1994, pp. 61-71
Avid AL is an affinity chromatographic gel based on a synthetic ligand
which has been designed for the purification of immunoglobulins. The
binding capacities of the gel for human IgG were investigated under di
fferent conditions; various salts; salt concentrations; different buff
er systems with pH ranging from 3.8 to 10.0; and, tissue culture super
natant supplemented with 20% serum. At a similar ionic strength, the b
inding capacity changed according to the salting out effect of the ion
s used. Kinetic parameters of the affinity adsorption showed that a st
rong salting out effect significantly decreased the dissociation const
ant. Avid AL gel purified IgG from human serum with a capacity of 26.2
mg/ml gel using binding buffer containing sodium sulfate. Recombinant
Protein A gel was used as a control. In this study it also exhibited
enhanced binding capacity with a high salt concentration binding buffe
r.