The effects of metal ions on esterase activities of urokinase.
The esterase activity of highly purified human urokinase on Nalpha-acetylglycl-L-lysine methyl ester is strongly inhibited by 1 X 10(-5) to 1 X 10(-2)M Cu++, Hg++, Ni++, Co++, Fe+++, and Mn++ solutions, whereas Na+, K+, Ca++, and Mg++ are weakly effective. This inhibition is parallel with the inhibition of activation of plasminogenby urokinase. There is no simple linear relation between inhibiton and concentration. Addition of ethylenediaminetetraacetate or electrodialysis fully reactivates the inhibited enzyme. These results are discussed in relation to similar effects of ions on trypsin.
D004151:Dipeptides / Q000378:metabolism; D004492:Edetic Acid; D010450:Endopeptidases / Q000378:metabolism*; D004791:Enzyme Inhibitors; D004950:Esterases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology*; D014357:Trypsin / Q000378:metabolism; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
D004151:Dipeptides; D004791:Enzyme Inhibitors; D008670:Metals; D004492:Edetic Acid; D004950:Esterases; D010450:Endopeptidases; D014357:Trypsin; D014568:Urokinase-Type Plasminogen Activator