Comparative properties of channel catfish (Ictalurus punctatus) and blue crab (Callinectes sapidus) acetylcholinesterases.
1. Acetylcholinesterases (AChEs) from channel catfish and blue crabs were examined for substrate preference, KmS, effects of inhibitors, and pH and osmotic activity profiles. 2. Similarities were noted for substrate preference along with pH and osmotic optima. 3. Crab AChE had a lower Km (9 x 10(-5) vs 2 x 10(-4) M) and was more sensitive in terms of KI50S than fish AChE to eserine (2.6 x 10(-7) vs 3 x 10(-7) M), malathion (4.5 x 10(-5) vs 1.6 x 10(-4) M) and parathion (6.9 x 10(-5) vs 7 x 10(-4) M). 4. Fish AChE appeared easier to solubilize using Triton X-100.
Habig
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C
School of Forestry and Environmental Studies, Duke University, Durham, North Carolina 27706.
Di Giulio
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RT
Abou-Donia
M B
MB
D000110:Acetylcholinesterase / Q000032:analysis*; D000818:Animals; D003386:Brachyura / Q000378:metabolism*; D002397:Catfishes / Q000378:metabolism*; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007059:Ictaluridae / Q000378:metabolism*; D007700:Kinetics; D009995:Osmosis; D013379:Substrate Specificity
D002800:Cholinesterase Inhibitors; D000110:Acetylcholinesterase