English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Horse urinary kallikrein was titrated with the reagent 4-nitrophenyl 4-guanidino-benzoate. The titration was shown to be dependent upon the concentration of the titrant. This finding, which distinguishes horse urinary kallikrein from other enzymes, is explained by the relatively small ratio between its rate of acylation and deacylation (k2/k3 = 16.8) and by a low affinity of the reagent (Km = 1.16 microM). By an appropriate kinetic treatment, it was possible to establish the relationship between the hydrolysis of 4-nitrophenyl 4-guanidinobenzoate and the actual concentration of the active enzyme.

Active-Site Titration of Horse Urinary Kallikrein