ENZYME CHEMICAL STUDIES ON CHOLINESTERASE IN DOG BRAIN, LIVER AND ERYTHROCYES
1980 Volume 40 Issue 1 Pages 69-74
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1980 Volume 40 Issue 1 Pages 69-74
Effects of inhibitors such as DFP and eserine, heat treatment and trypsin and triton x-100 treatment on cholinesterase (ChE) in dog brain and liver mitochondria and erythrocytes with acetyl-β-methylcholine (MeCh), butyrylcholine (BuCh) and tributyrin as substrate of true ChE, pseudo ChE and esterase, respectively were studied. pI 50's of DFP with brain ChE were 10-4.2 M in McCh, 10-7.2 M in BuCh and 10-5.2 M in tributyrin and with liver they were 10-7 M in BuCh and 10-7.2 M in tributyrin and with erythrocytes they were 10-3.5 M in McCh and similar to brain in BuCh and tributyrin. In case of eserine, pI 50's with brain were 10-7 in McCh, and 10-8 M in BuCh and 10-4 M in tributyrin and those with liver were almost similar to brain in BuCh and 10-3 M in tributyrin. In erythrocytes, they were similar to brain in McCh but when high concentration of eserine (10-3 M) was used, ChE activity was decreased to 50% in BuCh and no inhibition was observed in tributyrin. ChE activities of brain, liver and erythrocytes were disappeared within 4 minutes by heat treatment at 60°C with McCh and slight decrease was observed in 6 minutes with BuCh. By trypsin treatment for 30 minutes, ChE activities of brain and erythrocytes were decreased more than 80% with McCh and those of brain and liver were decreasd to 40% and 20% with BuCh, respectively. By treatment of 25% triton x-100, ChE was solubilized to 90% with McCh, 65% with BuCh in brain and to 90% with BuCh in liver.
