Effect of hypothermia on kinetic characteristics of acetylcholine esterase in rat erythrocyte membranes.
We studied kinetic and thermodynamic characteristics of acetylcholine esterase in rat erythrocyte membrane after whole-body hypothermia (20 degrees C) of different duration. Hypothermia increased the degree of substrate inhibition for acetylcholine esterase, maximum rate, and Michaelis constant. The temperature dependence of acetylcholine esterase activity remained practically unchanged.
Klichkhanov
N K
NK
Laboratory of Ecological Biochemistry, Laboratory of Biophysics and Physiology, Institute of Biology, Dagestan State University, Makhachkala.
Meilanov
I S
IS
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D021461:Animals, Outbred Strains; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000378:metabolism*; D007036:Hypothermia, Induced; D007700:Kinetics; D008297:Male; D051381:Rats; D013696:Temperature
D000110:Acetylcholinesterase