title: Oxyhemoglobin inhibition of acetylcholinesterase activity.
abstract: The effects of human oxyhemoglobin (HbO2), human methemoglobin (MetHb), and porcine serum albumin (PSA) on the activity of acetylcholinesterase (AChE) isolated from Electrophorus electricus were examined. HbO2 produced a dose-dependent reduction in AChE activity. Fifty percent of activity was obtained at 5 microM HbO2, while 95% inhibition was obtained at 50 microM. In this concentration range MetHb and PSA had little effect on esterase activity.
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002800:Cholinesterase Inhibitors / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D004593:Electrophorus; D006801:Humans; D008706:Methemoglobin / Q000494:pharmacology; D010108:Oxyhemoglobins / Q000494:pharmacology*; D012709:Serum Albumin / Q000494:pharmacology; D013552:Swine
chemical_list: D002800:Cholinesterase Inhibitors; D010108:Oxyhemoglobins; D012709:Serum Albumin; D008706:Methemoglobin; D000110:Acetylcholinesterase