Conformational plasticity of IgG during protein A affinity chromatography
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文摘

IgG bound to protein A by mixed interactions, through one or both heavy chains.

IgG eluted from protein A at sizes descending to 2 nm, then increasing to 10 nm.

Reducing size was caused mostly by a mechanism independent from protein A.

The independent mechanism involved IgG concentration, low pH and conductivity.

Increasing size was caused by denaturation from interaction with 2 protein A domains.

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