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Rapid determination of immobilized ConA lectin activity

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Abstract

ConA was immobilized on an epoxy-activated copolymer of 2-hydroxyethyl-methacrylate and ethylene-dimethacrylate and commercially available high-pressure liquid chromatography (HPLC) sorbents Separon HEMA 1000 EL, Separon HEMA 1000 E, and Separon HEMA 1000 EH (Tessek, Prague, CSFR Denmark). Specific, sensitive, and rapid method for determination of immobilized ConA lectin activity was developed. β-Galactosidase fromAspergilus oryzae oligomannosyl residues was used as specific affinant. After separation of bound and unbound β-galactosidase, enzyme activity was measured in supernatant and thus immobilized ConA lectin activity was calculated easily. The use of the method for evaluating the properties of immobilized ConA, efficiency of immobilization, specific activity, and thermostability is shown. The method developed could be generalized by using artificially glycosylated enzyme for any lectin.

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Authors and Affiliations

  1. Research Institute of Rheumatic Diseases, Nábrežie Ivana Krasku 4, 921 01, Piesany, CSFR

    Eduard Orviský, Vladimír Kéry, Katarińa Vandáková & Mária Stančíková

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  1. Eduard Orviský
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  2. Vladimír Kéry
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  3. Katarińa Vandáková
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  4. Mária Stančíková
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Orviský, E., Kéry, V., Vandáková, K. et al. Rapid determination of immobilized ConA lectin activity. Appl Biochem Biotechnol 32, 127–134 (1992). https://doi.org/10.1007/BF02922153

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  • DOI: https://doi.org/10.1007/BF02922153

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