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Results 1 - 10 of 12 > >>
EC Number pH Stability pH Stability Maximum Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.72-999 - effect of pH on conformation 31481
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.724 12 pre-incubation of fibrinolytic protease for 1 h at pH 4.0-12.0 causes substantial activity loss 733238
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.725 11 the enzyme remains stable for 2 h at pH 5.0-11.0, retaining more than 80% activity 754441
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.725.5 - 6 h, 30-35% loss of activity 31471
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.725.8 9.2 protease and fibrinolytic activities are stable during 6 h, at a pH ranging from 6.8 to 8.4 and 5.8 to 9.2, respectively 752378
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.726 12 the enzyme activity remains stable after 60 min at pH 6.0-12.0 753870
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.726 12 the purified enzyme shows higher stability between pH 6.0-8.0 retaining more than 90% of its activity while it retains 87.22 and 74.23% of its activity at pH 5.0 and 9.0, respectively. With further increase in pH 18% residual activity is observed at pH 12.0 752343
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.726.5 - optimal pH for stability 31471
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.726.5 10 stable 31481
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.727 - after incubation for 12 h, the enzyme retains 82.89% of its activity at pH 7.0, 66.03% at pH 8.0, and 50% at pH 6.0 and 9.0 after 8 h of incubation, respectively 754580
Results 1 - 10 of 12 > >>