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
✦ LIBER ✦
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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