title: Some properties of human pancreatic kallikrein and comparison with human trypsins and porcine kallikrein.
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.
mesh_terms: D000818:Animals; D006801:Humans; D007610:Kallikreins / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine; D014357:Trypsin / Q000378:metabolism*
chemical_list: D007610:Kallikreins; D014357:Trypsin