, Volume 35, Issue 1–2, pp 93–96 | Cite as

Purification of125I-labelled aprotinin by hydrophobic interaction chromatography

  • G. Raspi
  • A. Lo Moro
  • M. Spinetti


125I-aprotinin has been prepared and purified by affinity chromatography in combination with hydrophobic interaction chromatography (HIC). The method allows the preparation of the labelled inhibitor practically carrier-free, in saline solution without organic modifier and the isolated compound retained inhibition activity. Recovery of radioactive material was virtually quantitative, without substantial accumulation of radioactivity on the column. Compared with currently used procedures, the method is more reliable because the labelled polypeptide is collected by following its specific chromatographic signal.

Key Words

Liquid chromatography Bovine pancreatic trypsin inhibitor 125I-labelled compounds 


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Copyright information

© Friedr. Vieweg & Sohn Verlagsgesellschaft mbH 1993

Authors and Affiliations

  • G. Raspi
    • 1
  • A. Lo Moro
    • 1
  • M. Spinetti
    • 1
  1. 1.Dipartimento di Chimica e Chimica IndustrialeUniversità di PisaPisaItaly

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