, Volume 34, Issue 4, pp 275–280 | Cite as

Aprotinin, a carbohydrate-binding protein

  • R. W. Stoddart
  • J. A. Kiernan


Evidence is presented for a carbohydrate-binding property of aprotinin, which is preserved both in a fluorescein isothiocyanate (FITC) conjugate and a cyanogen bromidelinked Sepharose conjugate of the protein. Both conjugates similarly retain their tryptic and chymotryptic inhibitory properties. The FITC conjugate is shown to be a single species with respect to charge and to molecular weight and shows a specific binding of normal materials containing sialosyl or uronosyl groups, which accords with its histochemical behaviour. The Sepharose-conjugate showed a similar specificity.


Public Health Molecular Weight Fluorescein FITC Specific Binding 
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Copyright information

© Springer-Verlag 1973

Authors and Affiliations

  • R. W. Stoddart
    • 1
  • J. A. Kiernan
    • 2
  1. 1.Strangeways Research LaboratoryCambridgeUK
  2. 2.Dept. of AnatomyUniversity of CambridgeCambridgeUK

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