Rat urinary kallikrein was separated by high-performance liquid chromatography (HPLC) using an ion-exchange or gel-permeation column. Kallikrein activity was monitored continuously with peptidase or esterase activity using a post-reactor system directly adapted to HPLC. A PTFE helically coiled tube served as the enzyme reactor vessel. Four and three peaks with peptidase and esterase activity, respectively, were detected on application of normal rat urine. © 1983.
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