Abstract
Reactive carbonyl groups have been introduced into Sephadex and Sepharose gels by oxidation with aqueous bromine at pH 7. Proteins and other amines have been coupled in high yields to oxidized Sepharose gels by reductive amination. The reactions are carried out in aqueous solutions at pH 7 with sodium cyanoborohydride as a reducing agent. The biological activity of a tested immobilized enzyme (urokinase) is not altered. The effect of the oxidation-reduction procedure on the chromatographic properties of Sepharose gels in insignificant. The Sephadexes are much altered at high degrees of oxidation.
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