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The interaction ofClostridium perfringens sialidase with immobilized sialic acids and sialyl-glycoconjugates

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Abstract

Clostridium perfringens sialidase is adsorbed by sialic acid immobilized on adipic acid dihydrazido-Sepharose 4B and/or polymethylacrylic hydrazido-Sepharose 4B, through its carboxyl group, C-7 to C-9 side chain, or its amino function asd-neuraminic acid-β-methyl glycoside or 2-deoxy-2,3-didehydroneuraminic acid. Sialidase binding was strongest to the amino-linked adsorbents, but purification was low and the enzyme could not be eluted with substrate or free sialic acid. Low binding of the sialidase to the non-substituted, blocked supports suggested that hydrophobic interactions were involved, and this was confirmed by adsorption of the enzyme on alkyl agaroses with approximately 80% of total sialidase adsorbed on decyl-agarose. Genuine affinity chromatography of sialidases is possible on immobilized sialyl-glycoconjugates, andC. perfringens sialidase could be purified to the same specific activity as the electrophoretically homogeneous enzyme using submandibular gland mucus glycoprotein adsorbents. Sialidases fromVibrio cholerae, Arthrobacter ureafaciens, Newcastle disease virus, Fowl plague virus and Influenza A2 virus also bound to immobilized sialic acids and sialyl-glycocojugates.

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Author notes

  1. Anthony P Corfield

    Present address: Department of Medicine Laboratories, Bristol Royal Infirmary, BS2 8HW, Bristol, England

Authors and Affiliations

  1. Biochemisches Institut, Christian-Albrechts-Universität, Olshausenstr. 40, D-2300, Kiel, Germany

    Anthony P Corfield, Clarice do Amaral Corfield, Margret Wember & Roland Schauer

Authors
  1. Anthony P Corfield
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  2. Clarice do Amaral Corfield
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  3. Margret Wember
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  4. Roland Schauer
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Dedicated to Prof. Dr. Hans Faillard on the occasion of his 60th birthday.

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Corfield, A.P., Corfield, C.d.A., Wember, M. et al. The interaction ofClostridium perfringens sialidase with immobilized sialic acids and sialyl-glycoconjugates. Glycoconjugate J 2, 45–60 (1985). https://doi.org/10.1007/BF01225112

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  • DOI: https://doi.org/10.1007/BF01225112

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