Abstract
Utilization of 125I-labeled IgG enables an investigation of protein immobilized to gold electrodes sputter deposited on microporous nylon membranes, including the precise nature of the surface–protein bond (i.e. covalent or non-specific adsorption), physical location of the immobilized protein (i.e. on the surface of the gold electrode or within the pores of the membrane), and the amount of protein immobilized. This is accomplished by comparing the mass of protein immobilized to gold surfaces that have been treated in several different fashions, as well as, deposition of the gold on nylon membranes that have been treated differently. It is shown that these microporous gold electrodes, proposed previously for conducting novel non-separation electrochemical enzyme immunoassays, consist of multiple protein layers non-specifically adsorbed. Approximately, half of the total adsorbed protein is immobilized to the gold surface with the remaining protein bound within the pores on the nylon membrane.
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