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

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)235-239
Number of pages5
JournalAnalytical Biochemistry
Volume103
Issue number1
DOIs
Publication statusPublished - Mar 15 1980

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ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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