Mar 1, 1980

Biochemical Characterization of an Acetylcholine-hydrolyzing Enzyme from Bean Seedlings

Plant Physiology
M Ernst, E Hartmann

Abstract

An acetylcholine hydrolyzing enzyme was prepared and purified (40 times) from dwarf bean hypocotyl hooks. The purity of the enzyme was proved by polyacrylamide gel electrophoresis. The molecular weight of the enzyme was determined to be 65,000 daltons. Enzyme activity was the highest at pH 8.0 and between 30 and 36 C. The enzyme had an apparent affinity constant (K(m)) for acetylcholine of 460/micromolar. The affinity for substrate analogs increased from butyrylthiocholine to propionylthiocholine to acetylthiocholine. The enzyme activity was inhibited by choline, neostigmine, physostigmine, manganese, and calcium. Magnesium had no influence on the enzyme activity. We conclude that the enzyme from dwarf beans is an acetylcholinesterase (EC 3.1.1.7).

Mentioned in this Paper

Choline
Calcium [EPC]
Magnesium Measurement
Calcium
Analog
Butyrylthiocholine
Enzyme Activity
Blood Enzyme Activity (Lab Test)
Esterases
Acetylthiocholine

About this Paper

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