Selected article for: "catalytic efficiency and kcat Km catalytic efficiency"
Author: Wysocki, Jan; Schulze, Arndt; Batlle, Daniel
Title: Novel Variants of Angiotensin Converting Enzyme-2 of Shorter Molecular Size to Target the Kidney Renin Angiotensin System
  • Document date: 2019_12_17
    • ID: 0vozochc_27
    Snippet: Clonal HEK293 cell lines stably expressing the two ACE2 variants (1-605 and 1-619) were established, and the recombinant proteins were purified from the culture medium by strong anion-exchange chromatography, as shown in Supplementary Figure S1A [see details in Methods]. Purified native rACE2 1-740 [7] was used as a control to compare the enzymatic activities of the two short ACE2 variants. The catalytic efficiency of the two short ACE2 variants .....
    Document: Clonal HEK293 cell lines stably expressing the two ACE2 variants (1-605 and 1-619) were established, and the recombinant proteins were purified from the culture medium by strong anion-exchange chromatography, as shown in Supplementary Figure S1A [see details in Methods]. Purified native rACE2 1-740 [7] was used as a control to compare the enzymatic activities of the two short ACE2 variants. The catalytic efficiency of the two short ACE2 variants (Kcat/Km) to cleave the synthetic fluorogenic ACE2 substrate, Mca-APK-(Dnp) [7] , was higher as compared to native rACE2.

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