Abstract
We present data to suggest that divinylsulphone-activated matrix (DVS-gel) purifies immunoglobulins with the same protein-ligand interaction as the thiophilic ligand, T-gel. Divinylsulphone-activated matrix purifies IgG (>90% pure) from blood serum with a binding capacity of 6.3 mg/ml, compared to 6.9 mg/ml with T-gel. It also separates IgG and sIgA from cheese whey, with the same dependency on water-structuring salt concentration as T-gel. We offer an explanation for these results in terms of the polymerisation of divinylsulphone and, therefore, offer a new structure for the so-called thiophilic ligand.
Published Version
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