Abstract
Summary
A variety of commonly employed membrane solubilizing agents were studied for a possible effect on erythrocyte AChE activity. Only sodium deoxycholate had any appreciable inhibitory effect.
Stepwise solubilization of red cell membrane with a variety of agents showed no selective removal of membrane AChE. Rather the release of enzymic activity closely paralleled the solubilization of membrane proteins, suggesting that AChE is an integral part of the membrane.
A relatively simple method was described for the isolation and purification of human red cell AChE which resulted in a 4200-fold purification. The enzyme appears to be associated with lipids and gave a single precipitin band on immunodiffusion.
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