Maleimide-activated immunoglobulins

The isoterms of adsorption of maleimide-activated immunoglobulins on the surface of Fe304/DMSA were investigated. The adsorption capacity value was A=92.12mg/g (Table 10.7), with the specific surface area specific = 130 m /g. The release of immunoglobulin, immobilized by means of sulfo-SMCC spacer, in the model medium was 8—12% for 24 h. 

The number of sulfhydryls created on the immunoglobulin using thiolation procedures such as this one is more critical to the yield of conjugated enzyme molecules than the molar excess of maleimide-activated enzyme used in the conjugation reaction. Therefore, it is important to use a sufficient excess of Traut s reagent to obtain a sufficient number of available sulfhydryls. 

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