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Salting-out adsorption techniques for protein purification

✍ Scribed by Jerker Porath

Publisher
Wiley (John Wiley & Sons)
Year
1987
Tongue
English
Weight
749 KB
Volume
26
Category
Article
ISSN
0006-3525

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✦ Synopsis

Synopsis

Salt-promoted adsorption of proteins occurs on hydrophobic gels, on immobilized metal ions e.g., Znz+, C g + , Ni2+, Cu2+, and on newly described absorbents provisionally called "thiophilic gels." The latter gels are characterized by the ligand structure -SO,-CH,-CH,-S-R.

In a simple form (R = -CH,-CH,-OH) the 'IT-gel" is extremely useful for rapid isolation of immunoglobulins from complex mixtures. When R is rich in ?r-electrons the thiophilic affinity will be superimposed by charge-transfer coupling with hitherto unknown counterligands in interacting proteins. The use of tandem and cascade processes for protein fractionation according to several more or leas independent separation parameters is briefly demonstrated.

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