The characteristics of the inhibition of serum cholinesterase by metoclopramide
β Scribed by S. G. Graham; A. W. A. Crossley
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 393 KB
- Volume
- 48-48
- Category
- Article
- ISSN
- 0031-6970
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β¦ Synopsis
The inhibition of serum cholinesterase by metoclopramide has been previously characterised in vitro at high dilution of the enzyme. We examined the effect of varying enzyme dilution over a range of 1000 fold dilution, and assay temperature at 25Β°C and 37Β°C on the fractional inhibition of enzyme activity by metoclopramide. Neither enzyme concentration nor reaction temperature affected this fractional inhibition. Concentrations of metoclopramide producing 50% inhibition of enzyme activity were in the range 1.0-1.9 Γ 10 -6 M. Lineweaver-Burk analysis of the enzyme reaction suggests that the pattern of this inhibition is competitive.
π SIMILAR VOLUMES
## Abstract Metoclopramide (MCP) is a dopamine receptor antagonist and serotonine receptor agonist widely used as an antiemetic and gastric prokinetic drug. In addition MCP is a reversible inhibitor of cholinesterases from human central nervous system and blood. MCP may have a cholinesterase protec
## Abstract Metoclopramide (MCP) is a dopamine receptor antagonist and serotonin receptor agonist widely used as an antiemetic and gastric prokinetic drug. In addition MCP is a reversible inhibitor of cholinesterases from human central nervous system and blood. Metoclopramide may have a cholinester