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Effect of Mg2+-ATP on Acetylcholinesterase of Electrophorus electricus (L.)

A. Nery da Matta, C. B. Silva, A Hassón-Voloch

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Abstract

The effect of Mg(2+)-ATP on purified acetylcholinesterase (AChE) from electric tissue of Electrophorus electricus (L.) was studied. The enzymatic activities were measured with acetylcholine and acetylthiocholine as substrates. The kinetic parameters Vmax, Km and Hill coefficient (nH), for acetylcholine and acetylthiocholine were modified with Mg(2+)-ATP. It was shown that acetylcholinesterase presents an apparent activation at high concentration of substrates and an inhibition in the presence of Mg(2+)-ATP at low concentration of acetylcholine and acetylthiocholine. In addition, the data suggest that Mg(2+)-ATP induced an allosteric modulation of the acetylcholinesterase obtained from Electrophorous electricus (L.), and indicate an active adenosine triphosphate participation during cholinergic activity.

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The effect of Mg(2+)-ATP on purified acetylcholinesterase (AChE) from electric tissue of Electrophorus electricus (L.) was studied. The enzymatic activities were measured with acetylcholine and acetylthiocholine as substrates. The kinetic parameters Vmax, Km and Hill coefficient (nH), for acetylcholine and acetylthiocholine were modified with Mg(2+)-ATP. It was shown that acetylcholinesterase presents an apparent activation at high concentration of substrates and an inhibition in the presence of Mg(2+)-ATP at low concentration of acetylcholine and acetylthiocholine. In addition, the data suggest that Mg(2+)-ATP induced an allosteric modulation of the acetylcholinesterase obtained from Electrophorous electricus (L.), and indicate an active adenosine triphosphate participation during cholinergic activity.

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Available abstract

The effect of Mg(2+)-ATP on purified acetylcholinesterase (AChE) from electric tissue of Electrophorus electricus (L.) was studied. The enzymatic activities were measured with acetylcholine and acetylthiocholine as substrates. The kinetic parameters Vmax, Km and Hill coefficient (nH), for acetylcholine and acetylthiocholine were modified with Mg(2+)-ATP. It was shown that acetylcholinesterase presents an apparent activation at high concentration of substrates and an inhibition in the presence of Mg(2+)-ATP at low concentration of acetylcholine and acetylthiocholine. In addition, the data suggest that Mg(2+)-ATP induced an allosteric modulation of the acetylcholinesterase obtained from Electrophorous electricus (L.), and indicate an active adenosine triphosphate participation during cholinergic activity.

Key concepts: Electrophorus, Acetylthiocholine, Acetylcholinesterase, Acetylcholine, Chemistry, Allosteric regulation, Biophysics, Adenosine triphosphate

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