Title : Cooperative inhibition of acetylcholinesterase activities by hexachlorophene in human erythrocytes.

Pub. Date : 1997

PMID : 9049051






5 Functional Relationships(s)
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1 Cooperative inhibition of acetylcholinesterase activities by hexachlorophene in human erythrocytes. Hexachlorophene acetylcholinesterase (Cartwright blood group) Homo sapiens
2 The inhibition of AchE activities by HCP was reversed on adding albumin. Hexachlorophene acetylcholinesterase (Cartwright blood group) Homo sapiens
3 On a Scatchard plot analysis, erythrocyte membranes appeared to have multiple binding sites of different affinities for HCP; binding of HCP to the low affinity site [dissociation constant (Kd) 4.7 x 10(-5) M] seemed to be responsible for the observed cooperative inhibition of AchE activities. Hexachlorophene acetylcholinesterase (Cartwright blood group) Homo sapiens
4 HCP seems to be the most potent cooperative inhibitor of AchE in human erythrocyte membranes known to date. Hexachlorophene acetylcholinesterase (Cartwright blood group) Homo sapiens
5 HCP may be useful to examine AchE and milieu in human erythrocyte membranes. Hexachlorophene acetylcholinesterase (Cartwright blood group) Homo sapiens