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Purification of human serum albumin by affinity chromatography

1974; Elsevier BV; Volume: 372; Issue: 1 Linguagem: Inglês

10.1016/0304-4165(74)90088-9

1872-8006

Anders Wichman, L. Andersson,

Protein Interaction Studies and Fluorescence Analysis

The ability of serum albumin to bind various long-chain fatty acids has been utilized in the development of a specific adsorbent for albumin. Various alkyl succinic acids were coupled to agarose gel through diaminoalkane spacers. The gels obtained strongly adsorbed human serum albumin. The bound albumin could be desorbed by elution with sodium dodecylsulphate or in some cases sodium caprylate. The binding strength was dependent both on the length of the alkyl chain in the alkyl succinic acid and on the size of the spacer. Using one adsorbent and suitable elution conditions it was possible to isolate human serum albumin directly from plasma in a purity exceeding 99%. Gradient elution of adsorbed serum albumin with sodium caprylate resulted in partial separation of various mercapt- and nonmercaptalbumin components.