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Histochemie

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

Aprotinin, a carbohydrate-binding protein

  • R. W. Stoddart
  • J. A. Kiernan
Article

Summary

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.

Keywords

Public Health Molecular Weight Fluorescein FITC Specific Binding 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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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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