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Separation of aspartate aminotransferase from albumin on substituted agaroses

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Abstract

The affinity of aspartate aminotransferase to its inhibitors coupled to Sepharose 4 B was tested. The affinity was measured as retardation of the enzyme compared to “inert” bovine serum albumin. Carboxylic ligands of citrate and 2-oxoglutarate bound to aminoethyl-Sepharose were the best of those tested in separation of the proteins. Because the ligands were not essentially hydrophobic and because it was shown that ion-exchange is not significant in the elution conditions used, it was suggested that the separation is based on the recognition of substrate or effector by the enzyme.

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Authors and Affiliations

  1. Department of Biochemistry, University of Turku, SF-20500, Turku 50, Finland

    T. K. Korpela, E. I. Kukko & A. E. Hinkkanen

Authors
  1. T. K. Korpela
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  2. E. I. Kukko
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  3. A. E. Hinkkanen
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Korpela, T.K., Kukko, E.I. & Hinkkanen, A.E. Separation of aspartate aminotransferase from albumin on substituted agaroses. Journal of Solid Phase Biochemistry 3, 215–221 (1978). https://doi.org/10.1007/BF02991848

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  • DOI: https://doi.org/10.1007/BF02991848

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