NEUROTRANSMITTER-RELATED ENZYME ACETYLCHOLINESTERASE IN JUVENILES OF CONCHOLEPAS-CONCHOLEPAS (MOLLUSCA, GASTROPODA, MURICIDAE)
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Date
1990
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Abstract
With the aim of understanding the organization of the nervous systemn in the Prosobranchia gastropod Concholepas concholepas, we studied the properties, specificity, sedimentation coefficient, and solubility of the cholinergic enzyme, acetylcholinesterase (AChE). It was found that 95% of the esterase was inhibited by BW284c51 dibromide but not by iso-OMPA, which is consistent with the specificity of AChE. The calculated Km 0.22 mM is eight to ten times higher than are the Kms for AChE of other invertebrates and similar to the values reported for fish and vertebrates. The AChE shows a maximal activity around 22.degree. C, has a glycoprotein character and presents sedimentation coefficients of 6.5 S and 10.5 S. Most of this AChE activity is soluble under low ionic strength conditions; however, the enzyme aggregates in the absence of detergents. In conclusion, our evidence indicates the presence of a well-recognized molecular marker that could be useful for the study of the development of Concholepas concholepas.