1991Biologia PlantarumOpen access

Acetylcholinesterase from oat Seedlings. I. Preliminary biochemical characterization of the enzyme

Jacek Kęsy, Andrzej Tretyn, H Łukasiewicz, Jan Kopcewicz

Open full text 3 citations

Abstract

The activity of acetylcholinesterase (AChE) isolated from coleoptiles of etiolated oat seedlings is strongly inhibited by neostigmine and less so by eserine. The optimum of the enzyme activity occurs at pH 7.2 and a temperature of + 36 °C. The enzyme Michaelis constant is 280 μM. Choline within the range of concentration from 0.001 to 10 mM does not affect the enzyme activity. Calcium ions at 5 mM concentration cause inhibition, while magnesium and manganese ions do not affect the enzyme activity.AChE isolated from oat seedlings differs in a number of properties from AChE occurring in the tissues of other plants.

Open-access reader

About this research paper

What this paper is about

The activity of acetylcholinesterase (AChE) isolated from coleoptiles of etiolated oat seedlings is strongly inhibited by neostigmine and less so by eserine. The optimum of the enzyme activity occurs at pH 7.2 and a temperature of + 36 °C. The enzyme Michaelis constant is 280 μM. Choline within the range of concentration from 0.001 to 10 mM does not affect the enzyme activity. Calcium ions at 5 mM concentration cause inhibition, while magnesium and manganese ions do not affect the enzyme activity.AChE isolated from oat seedlings differs in a number of properties from AChE occurring in the tissues of other plants.

Why it matters

OpenAlex reports 3 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

The activity of acetylcholinesterase (AChE) isolated from coleoptiles of etiolated oat seedlings is strongly inhibited by neostigmine and less so by eserine. The optimum of the enzyme activity occurs at pH 7.2 and a temperature of + 36 °C. The enzyme Michaelis constant is 280 μM. Choline within the range of concentration from 0.001 to 10 mM does not affect the enzyme activity. Calcium ions at 5 mM concentration cause inhibition, while magnesium and manganese ions do not affect the enzyme activity.AChE isolated from oat seedlings differs in a number of properties from AChE occurring in the tissues of other plants.

Key concepts: Acetylcholinesterase, Enzyme assay, Enzyme, Coleoptile, Chemistry, Aché, Etiolation, Biochemistry

Related papers

Back to paper searchBrowse research topicsOriginal source
Acetylcholinesterase from oat Seedlings. I. Preliminary biochemical characterization of the enzyme — Research Paper | ScholarLens