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The effect of the plasma membrane on the activity of angiotensin-I converting enzyme (ACE) plays a crucial role in the evaluation of food-derived ACE inhibitory peptides, although these peptides are commonly evaluated in the system with ACE in its free state. In this study, we constructed an in vitro membrane-bound ACE C domain system to simulate the presence of the plasma membrane. The resultant Km and Vmax suggested that the presence of the membrane reduced the affinity between ACE C domain and hippuryl-histidyl-leucine, while it incr
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