Effect of Mg(2+)-ATP on acetylcholinesterase of Electrophorus electricus (L.).
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.
Nery da Matta
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A
Departamento de Biologia Celular e Molecular, Universidade Federal Fluminense, Niteroi, RJ, Brasil.
Silva
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CB
Hassón-Voloch
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A
D000109:Acetylcholine / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D002846:Chromatography, Affinity; D004557:Electric Organ / Q000201:enzymology*; D004593:Electrophorus; D007700:Kinetics; D015636:Magnesium Chloride / Q000494:pharmacology; D013379:Substrate Specificity
D015636:Magnesium Chloride; D000255:Adenosine Triphosphate; D000109:Acetylcholine