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- W2053931883 abstract "The interaction of lactate dehydrogenase (LDH, EC 1.1.1.28) with triazine dyes spacer-linked to beaded cellulose was studied. The lenth of the spacer influences neither the binding capacity of the dye-affinity adsorbent nor the elution of the enzyme by NAD—sulphite. However, the length of the extension arm strongly affects the elution of LDH by salt. The results with beaded cellulose carrying butyl, hexyl and decyl residues point to pure hydrophobic interaction with LDH. The introduction of a terminal amino or carboxylic group in the aliphatic chain changes significantly the binding and elution behaviour of the enzyme. It is assumed that in addition to specific interactions realized by the dye chromophore and specific domains on the surface of the enzyme the spacer arm generates a second type of binding force which points to hydrophobic interactions. The latter might be the result of specific orientation governed by the dye-ligand—protein interaction." @default.
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- W2053931883 date "1990-06-01" @default.
- W2053931883 modified "2023-09-26" @default.
- W2053931883 title "New aspects of dye-ligand affinity chromatography of lactate dehydrogenase applying spacer-mediated beaded cellulose" @default.
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- W2053931883 doi "https://doi.org/10.1016/s0021-9673(01)93752-5" @default.
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