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- W107541134 abstract "1.|The preparation of a sensitive, synthetic substrate for urokinase α-N-acetylglycyl-l-lysine methyl ester has been described. 2.|The apparent Km and Vmax values for urokinase, thrombin (EC 3.4.4.13) and plasmin (EC 3.4.4.14) catalysed hydrolysis of this substrate have been determined. 3.|Soybean trypsin inhibitor and Trasylol at concentration which strongly inhibit the plasmin and trypsin catalysed hydrolysis of α-N-acetylglycyl-l-lysine methyl ester have been found to be without effect on urokinase or thrombin. 4.|The Ki values for ε-aminocaproic acid and aminomethyl-cyclohexanoic acid which act as competitive inhibitors of the urokinase catalysed hydrolysis of α-N-acetylglycyl-l-lysine methyl ester have been determined at pH 7.0 and 7.85. The Ki for aminomethyl-cyclohexanoic acid at pH 7.00 is 10 times as large as the Ki for ε-aminocaproic acid at this pH but at pH 7.85 the Ki values for the two inhibitors only differ by a factor of 2. The implications of these findings are discussed." @default.
- W107541134 created "2016-06-24" @default.
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- W107541134 date "1967-01-01" @default.
- W107541134 modified "2023-09-26" @default.
- W107541134 title "The hydrolysis of methyl ester by urokinase" @default.
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- W107541134 doi "https://doi.org/10.1016/0005-2744(67)90196-9" @default.
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