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  • Title: Some properties of human pancreatic kallikrein and comparison with human trypsins and porcine kallikrein.
    Author: Amouric M, Figarella C.
    Journal: Hoppe Seylers Z Physiol Chem; 1980; 361(2):85-90. PubMed ID: 6898514.
    Abstract:
    The properties of human pancreatic kallikrein purified from pancreatic juice were investigated. The enzyme is very stable at pH 8 but is rapidly inactivated at pH 2.6. It is a glycoprotein with a molecular weight of 35 000 as determined by gel filtration on Sephadex G-200. Contrary to the two human trypsins, human kallikrein like porcine pancreatic kallikrein is unable to hydrolyse casein and Met-Lys-bradykinin. Human pancreatic kallikrein is inactivated by diisopropyl fluorophosphate but not by chloro (N-p-toluolsulfonly-L-lysyl)methane. The enzyme does not react with various proteinase inhibitors (secretory pancreatic trypsin inhibitors, ovomucoid, lima bean and soybean trypsin inhibitors) but is inhibited by the Kunitz pancreatic trypsin inhibitor.
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