These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Reversible inhibition of acetylcholinesterases of different origins by quaternary phosphonium compounds].
    Author: Brestkin AP, Brovko VS, Zhukovskiĭ IuG, Kolchanova NA, Mirzabaev EA.
    Journal: Zh Evol Biokhim Fiziol; 1986; 22(2):123-6. PubMed ID: 3716682.
    Abstract:
    Studies have been made on the reversible inhibition of acetylcholinesterase activity from the erythrocytes of man, horse and camel, the electric organ of the skate Torpedo marmorata and eel Electrophorus electricus, the venom of the snakes Naja naja and Vipera lebetina, the brain of the pigeon Columba livia by tetraphenyl-, triphenylalkyl- and tributyrylalkyl-phosphonium salts. The investigated phosphonium inhibitors exhibit an evident specificity in their action: they were more effective in inhibiting the acetylcholinesterase from human erythrocytes than that from the erythrocytes of horse and camel. These salts were more effective with respect to the acetylcholinesterase activity of the electric organ of the skate than that of the electric organ of the eel. Acetylcholinesterases from the venom of the snakes exhibited practically identical sensitivity to all the phosphonium compounds investigated. The present work is the first attempt to use quaternary phosphonium salts (the so-called "hydrophobic ions") in comparative enzymological investigation.
    [Abstract] [Full Text] [Related] [New Search]