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- W1991473002 abstract "1. Nonspecific adsorption of proteins to substituted agarose is a serious interference in affinity chromatography. Coupling of alkyl- or arylamines to CNBr-activated agarose, the most frequent technique of preparing affinity adsorbents with agarose, results in the formation of strong ion exchangers with an apparent pK of about 10 for a basic amidine nitrogen. Coupling of analogous hydrazides gives essentially uncharged agarose derivatives at physiological pH. 2. α-Lactalbumin and ovalbumin were found to bind tightly to alkylagaroses with hydrocarbon chains of 4–8 carbon atoms. The same proteins were not adsorbed by the corresponding alkyl hydrazide derivatives of agarose. Bovine serum albumin adsorbed to both, amine- as well as hydrazide-substituted alkyl-agaroses. 3. Leucine aminopeptidase showed no affinity for alkyl-agaroses but was bound strongly to tyramine-agarose with partial inactivation of the enzyme. Leucine aminopeptidase was not adsorbed by the hydrazide analogue of tyramine-agarose, the 4-hydroxyphenylacetyl hydrazide derivative. A detergent-like mode of action is assumed for alkyl- or arylamines coupled to activated agarose." @default.
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- W1991473002 date "1974-08-01" @default.
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- W1991473002 title "The mode of adsorption of proteins to aliphatic and aromatic amines coupled to cyanogen bromide-activated agarose" @default.
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- W1991473002 doi "https://doi.org/10.1016/0304-4165(74)90028-2" @default.
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