Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?

David Palesch, Marcin Sieńczyk, Jozef Oleksyszyn, Michael Reich, Ewa Wieczerzak, Bernhard O Boehm, Timo Burster

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.

Original languageEnglish
Pages (from-to)39-44
Number of pages6
JournalActa Biochimica Polonica
Issue number1
Publication statusPublished - 2011


  • Animals
  • Cathepsin G
  • Cattle
  • Cysteine Proteases
  • History, 20th Century
  • Mice
  • Rats
  • Spleen
  • Historical Article
  • Journal Article
  • Research Support, Non-U.S. Gov't

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