The mode of adsorption of proteins to aliphatic and aromatic amines coupled to cyanogen bromide-activated agarose.

作者: R. Jost , T. Miron , M. Wilchek

DOI: 10.1016/0304-4165(74)90028-2

关键词: Organic chemistryAmine gas treatingBovine serum albuminPolymer chemistryAmidineAlkylAgaroseHydrazideCyanogen bromideAffinity chromatographyChemistry

摘要: 1. 1. Nonspecific adsorption of proteins to substituted agarose is a serious interference in affinity chromatography. Coupling alkyl- or arylamines CNBr-activated agarose, the most frequent technique preparing adsorbents with results formation strong ion exchangers an apparent pK about 10 for basic amidine nitrogen. analogous hydrazides gives essentially uncharged derivatives at physiological pH. 2. 2. α-Lactalbumin and ovalbumin were found bind tightly alkylagaroses hydrocarbon chains 4–8 carbon atoms. The same not adsorbed by corresponding alkyl hydrazide agarose. Bovine serum albumin both, amine- as well hydrazide-substituted alkyl-agaroses. 3. 3. Leucine aminopeptidase showed no alkyl-agaroses but was bound strongly tyramine-agarose partial inactivation enzyme. analogue tyramine-agarose, 4-hydroxyphenylacetyl derivative. A detergent-like mode action assumed coupled activated

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