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Based on new material from Germany and Spain, the echinoid “Lepidocentrus” ibericusfrom the Early Devonian (Emsian) of northern Spain is shown to be congeneric with Rhenechinusfrom the Hunsrück Slate of south−western Germany. New information on the lantern, pedicellariae and internal structure of the theca is provided, and confirms this genus as a member of the Echinocystitidae–Proterocidaridae clade and the most primitive of all Devonian echinoids. The two environmental settings in which Rhenechinus is found are very different: the Spanish specimens come from a relatively shallow−water bryozoan meadow setting while the German specimens are preserved in a deep−water setting. We deduce that the rare echinoid specimens from the Hunsrück Slate are all allochthonous, whereas the Spanish material is preserved in situ.
 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.
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