Biochemical investigation of cholinesterase in the central nervous system of Lymnaea stagnalis L. (Gastropoda)

Varanka, István (1968) Biochemical investigation of cholinesterase in the central nervous system of Lymnaea stagnalis L. (Gastropoda). A Magyar Tudományos Akadémia Tihanyi Biológiai Kutatóintézetének évkönyve, 35. pp. 93-107. ISSN 0365-3005

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Abstract

Lymnaea stagnalis L. (Gastropod) and some biochemical properties of the enzyme were studied. I t could be stated that: 1 . The enzyme is active against cholinesters. The value of ACh hydrolysis by the homogenate is 33.0 mgACh/mg N/h. 2. The substrate pattern of the enzyme is: ACh 100%, BuCh 84%, PrCh 105%, MeCh 10% and BeCh 2%. Succinyl mono- and di-choline are not hydrolysed. 3. S-esters of ACh and BuCh are splitted to a lesser extent than their O-analogons. 4. pH optimum of enzyme activity with the use of ACh substrate is around: pH 9.0. 5. In cases of ACh and BuCh substrates the enzyme activity is inhibited with the increase of substrate concentration. pSopt of ACh is 1.81, th a t of BuCh is 1.70. 6. pI₅₀ values of the inhibition of enzyme activity are: for physostigmine with ACh substrate: 7.10, withPrCh substrate: 7.20; for neostigmine with ACh and PrCh substrates: 5.66; for DFP and TEPP with ACh substrates: 8.10 and 7.80 resp. 7. The enzyme is identified with acetylcholinesterase (acetylcholine acetyl-hydiolase, EC 3.1.1.7). 8. Biochemical evidences are suggested for the cholinergic mediation in the central nervous system in Lymnaea stagnalis.

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