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Cholinesterases from plant tissues. VI. Preliminary characterization of enzymes from Solanum melongena L. and Zea mays L.
Metadata
JournalBiochim. Biophys. ActaNot FoundDate
1975-Nov-20
Publication Type
Research Support, U.S. Gov't, Non-P.H.S.
Journal Article
Volume
1975-Nov-20 / 410 : 130-4
Author
Fluck RA , Jaffe MJ
DoiPMIDMESH
Acetylthiocholine
Cholinesterase Inhibitors
Cholinesterases
Hydrogen-Ion Concentration
Kinetics
Plants
Species Specificity
Structure-Activity Relationship
Subcellular Fractions
Zea mays
Abstract
Enzymes capable of hydrolyzing esters of thiocholine have been assayed in extracts of Solanum melongena L. (eggplant) and Zea Mays L. (corn). The enzymes from both species are inhibited by the anti-cholinesterases neostigmine, physostigmine, and 284c51 and by AMO-1618, a plant growth retardant and they both have pH optima near pH 8.0. The enzyme from eggplant is maximally active at a substrate concentration of 0.15 mM acetylthiocholine and is inhibited at higher substrate concentrations. On the basis of this last property, the magnitude of inhibition by the various inhibitors, and the substrate specificity, we conclude that the enzyme from eggplant, but not that from corn, is a cholinesterase.
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