May 1, 1975

Acetylcholinesterase from the electric organ of the ray Torpedo marmorata

Zhurnal evoliutsionnoĭ biokhimii i fiziologii
A P BrestkinL Rakic


Studies have been made on substrate specificity of acetylcholinesterase (AChE;EC 3-1-1-7) from the electric organ of the ray T. marmorata with respect of choline and thiocholine esters, as well as on the effect of pH, salts and organophosphorus inhibitors (OPI) on the activity of the enzyme. Acetylcholine (ACh), propionycholine (PrCh) acetyl-beta-methylcholine (MeCh), acetylthiocholine ((ATCh) and propionylthiocholine (PrTCh) were hydrolyzed by the enzyme studied at the following relative rates-100: 28.8: 18.3: 87.2: 18.9 correspondingly. In all the cases, inhibition of the enzyme by high concentrations of the substrate was observed. As compared to other AChE, the enzyme from T. marmorata exhibits the highest affinity to ACh. For all the substrates studied, pH dependence of AChE activity followed the curve with maximum 7.5 for ACh and PrCh, 8.0-8.5 for ATCh and MeCh and 7.5-8.5 for PrTCh. Various salts (MgCl2), KCl, NaCl, NaBr, KI) increased AChE activity, the increase being the highest with MgCl2 (3.3 times) and NaCl (2.5X). Biomolecular rate constants ((k) II) for the interaction of AChE investigated with OPI containing cationic group-methylsulfomethylates, O-ethyl-S-(beta-ethylmercapto) ethylmethylthiophosphonate and O,O-die...Continue Reading

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Mentioned in this Paper

Structure-Activity Relationship
Torpedo marmorata
Phosphate Measurement
Radicals (chemistry)
Plasma Protein Binding Capacity
Phosphorus Measurement

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