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LIPID PEROXIDE FORMATION IN RAT BRAIN
Lipid peroxide formation as measured by the thiobarbituric acid reaction was demonstrated in subcellular fractions of rat brain and the effect of thiol agents indicated that ‐SH groups were involved in the enzymic lipid peroxidation.
The aryl acylamidases and their relationship to cholinesterases in human serum, erythrocyte and liver.
Immunodiffusion and immunoprecipitation studies showed that the aryl acylamidases from the liver and erythrocytes were immunologically non-identical with the serum enzyme.
Noncholinergic functions of cholinesterases
- A. S. Balasubramanian, C. Bhanumathy
- BiologyFASEB journal : official publication of the…
- 1 November 1993
It appears that cholinesterases are capable of exhibiting more than one biological activity and their functions are wider than what is hitherto known.
Aryl acylamidase activity in human erythrocyte, plasma and blood in pesticide (organophosphates and carbamates) poisoning.
A CONTROLLED STUDY OF ENZYMIC ACTIVITIES IN THREE HUMAN DISORDERS OF GLYCOLIPID METABOLISM *
- J. Austin, A. S. Balasubramanian, T. N. Pattabiraman, S. Saraswathi, D. Basu, B. Bachhawat
- MedicineJournal of neurochemistry
- 1 November 1963
A CONTROLLED STUDY of ENZYMIC ACTIVlTIES in THREE HUMAN DISORDERS of GLYCOLIPID METABOLISM finds that zymic activities in three human diseases are connected.
The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from human erythrocytes, sheep basal ganglia and electric eel.
It is suggested that the serotonin-sensitive aryl acylamidase is identical with acetylcholinesterase, which was found to be highest for basal ganglia, less for erythrocyte and lowest for eel enzymes.
The association of the serotonin-sensitive aryl acylamidase with acetylcholinesterase in the monkey brain.
The serotonin-sensitive aryl acylamidase activity is a property of true cholinesterase and in the monkey brain the two activities may be associated with the same protein with two different active sites further experiments are needed to confirm this.
The inhibition of brain aryl acylamidase by 5-hydroxytryptamine and acetylcholine.
Chemical modification of the bifunctional human serum pseudocholinesterase. Effect on the pseudocholinesterase and aryl acylamidase activities.
- R. Boopathy, A. S. Balasubramanian
- Biology, ChemistryEuropean journal of biochemistry
- 1 September 1985
Modification by 2-hydroxy-5-nitrobenzyl bromide, N-bromosuccinimide, diethylpyrocarbonate and trinitrobenzenesulfonic acid caused a parallel inactivation of both pseudocholinesterase and aryl acylamidase activities that could be prevented by butyrylcholine iodide.
Evidence for a Zn(2+)-binding site in human serum butyrylcholinesterase.
The results suggest the presence of a Zn(2+)-binding site on human serum butyrylcholinesterase and the involvement of histidine residues in the metal binding.