Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence of high intake of vitamin C in the young growing rats under administration of nickel sulphate in toxic doses has been studied. Ingestion of nickel sulphate depresses the growth rates of rats, alters the vitamin C status in different tissues, inhibits certain enzymes of vitamin C metabolism and changes the activities of alkaline phosphatase and succinic dehydrogenase in the liver and kidney tissues. The acid phosphatase activity of liver, kidney and brain tissues of rats and glucose-6-phosphatase activity in liver, and serum GOT activity were stimulated, with reduction in the in the liver GOT activity. There is stimulation in the activities of rat brain inorganic pyrophosphatase and cholinesterase. Kidney tissues of rats were found to be more susceptible towards nickel toxicity as compared to the hepatic tissues in respect of morphological alterations. There is almost no alteration in the hepatic lipid composition. Administration of vitamin C in high doses to rats fed nickel salts in toxic doses can restore not only the growth rates but also certain enzyme activities to a significant extent.
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PMID:Biochemical studies on nickel toxicity in weanling rats -- influence of vitamin C supplementation. 23 Oct 18

It had been proposed that sialyl-residues on the surface of the cell control the activity of certain plasma membrane ecto-enzymes. We have tested the effects of several established (or presumptive) ecto-enzymes in tissue cultures of CNS-derived cells. Application of neuraminidases to cultured mouse neuroblastoma (N-18), neonatal Syrian hamster astrocytes (NN), human astrocytoma (Cox clone) and two lines of primary mouse astroblasts failed to change the activity of ecto-ATPase and 5'-nucleotidase. Only two of the seven neuraminidase preparations produced marked or moderate increases in inorganic pyrophosphatase, p-nitrophenylphosphatase and cholinesterase. We have concluded that the stimulation of these enzymes was not due to removal of sialyl-residues. We suggest that contaminants (haemolysins?) in neuraminidase preparations of Clostridium perfringens increased membrane permeability and facilitated substrate-product translocation.
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PMID:On the activation of plasma membrane ecto-enzymes by treatment with neuraminidase. 1217 May 85