Cholinesterases from Plant Tissues

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Cholinesterases from plant tissues: I. Purification and characterization of a cholinesterase from mung bean roots.

A cholinesterase was purified 36-fold from mung bean (Phaseolus aureus) roots by a combination of differential extraction media and gel filtration. The enzyme could be effectively extracted only by high salt concentration, indicating that it is probably membrane-bound. Methods used for assaying animal cholinesterases were tested, two of which were adapted for use with the bean cholinesterase. T...

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Cholinesterases from plant tissue: v. Cholinesterase is not pectin esterase.

Several properties of the cholinesterase from Phaseolus aureus Roxb. and of pectin (methyl) esterases from both Phaseolus aureus and Lycopersicon esculentum (L.) Mill. are contrasted. Cholinesterase activity is inhibited by all of the concentrations of NaCl tested, from 0.05 m to 0.9 m, a property which differs sharply from published data pertaining to pectin esterase. Although crude preparatio...

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Specific Sucrose Phosphatase from Plant Tissues

1. A phosphatase that hydrolyses sucrose phosphate (phosphorylated at the 6-position of fructose) was isolated from sugar-cane stem and carrot roots. With partially purified preparations fructose 6-phosphate, glucose 6-phosphate, fructose 1-phosphate, glucose 1-phosphate and fructose 1,6-diphosphate are hydrolysed at between 0 and 2% of the rate for sucrose phosphate. 2. The activity of the enz...

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Blood Cholinesterases from Washington State Orchard Workers

Court-ordered monitoring of blood cholinesterases (ChEs) from orchard workers in Washington State is underway. In 2008, the mean red blood cell acetylcholinesterase (AChE, EC 3.1.1.7) activity was 9.65 +/- 1.11 micromoles/min/ml (n = 1,793) and the mean serum (BChE, 3.1.1.6) activity was 5.19 +/- 0.90 micromoles/min/ml (n = 1,811). Determinations were made using the Ellman assay and automated e...

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Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618).

2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine carboxylate methyl chloride (AMO-1618) inhibits the activity of a cholinesterase isolated from mung bean (Phaseolus aureus) roots at concentrations comparable to those which retard growth and inhibit development of secondary roots of bean seedlings. Fifty per cent inhibition of the cholinesterase activity occurred at 0.21 mm. Inhibition of...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1973

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.52.3.233