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- W2040501322 abstract "Abstract 1. 1. In confirmation of the results of Mendel and Rudney, it has been shown that the optimum acetylcholine concentration for true cholinesterase is shifted to progressively higher levels by the addition of increasing concentrations of salt to the medium. 2. 2. The theoretical equations for Murray and Haldane have been applied to the resulting curves between enzyme activity and substrate concentration. It has been found that these equations will not fit the experimental results unless the assumption is made that the “inactive” complex ES 3 is subject to slow hydrolysis. The relative activity of the ES 2 complex would appear to be about one-tenth of the activity of the ES complex between enzyme ( E ) and substrate ( S ). 3. 3. The addition of simple salts (e.g., NaCl, KCl) decreases the affinity of true cholinesterase for acetylcholine. The salts have a further effect in potentiating the hydrolytic activity of true cholinesterase toward acetylcholine; this activation is especially marked with a bivalent salt such as calcium chloride. The significance of these results has been discussed in relation to the theory of a dipositional enzyme active center. 4. 4. The results support the supposition that the active center of the pseudocholinesterase is also dipositional in nature but the affinity of acetylcholine for pseudocholinesterase appears to be dependent mainly on the ester structure of the acetylcholine molecule." @default.
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- W2040501322 date "1952-06-01" @default.
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- W2040501322 title "Effect of salt on the hydrolysis of acetylcholine by cholinesterases" @default.
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- W2040501322 doi "https://doi.org/10.1016/0003-9861(52)90208-7" @default.
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