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.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.