Cholinesterase activity in the central nervous system of Anodonta cygnea L.

Salánki, János and Hiripi, László and Lábos, Elemér (1966) Cholinesterase activity in the central nervous system of Anodonta cygnea L. A Magyar Tudományos Akadémia Tihanyi Biológiai Kutatóintézetének évkönyve, 33. pp. 143-150. ISSN 0365-3005

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Abstract

The cholinesterase activity of the central nervous system of Anodonta cygnea (Pelecypoda) was investigated by biochemical methods. The cholinesterase activity observed is characterized by the followings: 1. ACh decomposition does not show linear increase parallel with the rise of substrate-concentration. 2. ACh-decomposition is most definite. 3. Acetyl-β-methylcholine (MeCh) decomposition is considerable. 4. There is no benzoylcholine decomposition. 5. 50% inhibition by 10⁻⁶ M eserine and by 10⁻⁷M DFP. 6. There is an optimum at pH 7, and a considerable decrease in activity below pH 6 and above pH 8. 7. An about 50% decrease in activity after one hour treatment in 4% formaldehyde. The above results indicate that a specific cholinesterase exists in the homogenized samples of the cerebral, visceral and pedal ganglia. At pH 8, at 37°C temperature and in case of 4 mM substrate concentration the rate of activity is 226 pg ACh /mg 1ST/ 1 hour, which is equivalent to about 1.8-2.2 mg ACh/1 hour/1 g wet-weight. The results suggest that cholinergic synapses may also be present in the ganglia of Anodonta. The low rate of decomposition and other factors indicate that they constitute only the smaller part of synapses in this animal and probably the central mechanisms are realized by chemical transmitters different from ACh.

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