Biochemical Characterization of an Acetylcholine-hydrolyzing Enzyme from Bean Seedlings.

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).

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Ernst M,Hartmann E

doi

10.1104/pp.65.3.447

subject

Has Abstract

pub_date

1980-03-01 00:00:00

pages

447-50

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

65

pub_type

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