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

Paolo Ascenzi; Alberto Bertollini; Daniela Verzili; Maurizio Brunori; Eraldo Antonini

doi:10.1016/0003-2697(80)90262-6

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

Paolo Ascenzi, Alberto Bertollini, Daniela Verzili, Maurizio Brunori, Eraldo Antonini

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article

Abstract

The catalytic properties of human urokinase have been investigated using a synthetic chromogenic substrate; α-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 (33,000 and 54,000 daltons), have been determined over the pH range 5.2-7.8, and found to be indistinguishable.

Original language	English
Pages (from-to)	235-239
Number of pages	5
Journal	Analytical Biochemistry
Volume	103
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(80)90262-6
Publication status	Published - Mar 15 1980

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ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

Cite this

Ascenzi, P., Bertollini, A., Verzili, D., Brunori, M., & Antonini, E. (1980). The hydrolysis of α-CBZ-l-lysine-p-nitrophenyl ester by two forms of human urokinase. Analytical Biochemistry, 103(1), 235-239. https://doi.org/10.1016/0003-2697(80)90262-6

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10.1016/0003-2697(80)90262-6