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 Physioljournal_title
Plant physiologyauthors
Ernst M,Hartmann Edoi
10.1104/pp.65.3.447subject
Has Abstractpub_date
1980-03-01 00:00:00pages
447-50issue
3eissn
0032-0889issn
1532-2548journal_volume
65pub_type
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