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The hydrolysis of α-CBZ-l-lysine-p-nitrophenyl ester by two forms of human urokinase

✍ Scribed by Paolo Ascenzi; Alberto Bertollini; Daniela Verzili; Maurizio Brunori; Eraldo Antonini


Publisher
Elsevier Science
Year
1980
Tongue
English
Weight
360 KB
Volume
103
Category
Article
ISSN
0003-2697

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✦ Synopsis


The catalytic properties of human urokinase have been investigated using a synthetic chromogenic substrate; a-CBZ-L-lysine-p-nitrophenyl ester (ZLNP). The enzymatic assay based on the rate of hydrolysis of ZLNP offers several advantages over other methods currently employed in different laboratories. The steady state parameters of the two purified forms of human urokinase, which differ in molecular weight (33,OOO and 54,OOO daltons), have been determined over the pH range 5.2-7.8, and found to be indistinguishable.


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The determination of human plasminogen u
✍ Robert M. Silverstein 📂 Article 📅 1975 🏛 Elsevier Science 🌐 English ⚖ 426 KB

An assay for human plasminogen using NU-CBZ-L-lysine p-nitrophenyl ester as the substrate is described. The procedure is performed by activating the sample with streptokinase for 5 min at pH 6.0 and 25", the substrate is added to this mixture and its hydrolysis is monitored spectrophotometrically at