Abstract
Seventeen N-alkyl substituted analogues of acetylcholine were tested as substrates for cholinesterase from housefly head and two-spotted spider mite. The housefly enzyme hydrolyzed the dimethyl and diethyl alkyl analogues rapidly whereas the activity to the dipropyl and dibutyl alkyl ester was low. With the mite enzyme no clear pattern of specificity to the esters was obtained. The propylene and butylene analogues of acetylcholine were hydrolyzed differently by the enzyme from the two sources.
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