Acetylcholinesterase in the brain of the marine gastropod Murex trunculus L. (Prosobranchia). Isolation and properties

• 1.1. Cholinesterase (ChE) of two types—acetylcholinesterase (AChE, acetylcholine hydrolase, EC 3.1.1.7) and propionylcholinesterase (PrChE, acylcholine hydrolase, EC 3.1.1.8)—was found in the brain of the marine gastropod Murex trunculus L. (Prosobranchia).
• 2.2. PrChE is a soluble enzyme which can be easily extracted by salt solution after freezing-thawing of the untreated brain.
• 3.3. AChE is membrane-bound. It was solubilized by a 0.2% solution of Triton X-100.
• 4.4. Some part of AChE (up to 36%) can spontaneously pass into solution.
• 5.5. The specific activity of AChE in Triton X-100 extracts is 100 ± 10 nmol acetylcholine/mg protein/min.
• 6.6. Enzyme hydrolysis of acetylcholine (ACh), acetylthiocholine (ATCh) and propionylthiocholine (PrTCh) is suppressed by excess of substrate. Michaelis constants (K_m) for their hydrolysis by AChE are 0.33, 0.017 and 0.018 mM, respectively.
• 7.7. Bimolecular rate constants with organophosphorus inhibitors of different structure points to a similarity of the gastropod brain AChE to the typical enzyme of vertebrates in the structure of the active surface.