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3.1.1.8: cholinesterase

This is an abbreviated version!
For detailed information about cholinesterase, go to the full flat file.

Word Map on EC 3.1.1.8

Reaction

an acylcholine
+
H2O
=
choline
+
a carboxylate

Synonyms

acyl choline acylhydrolase, acylcholine acyl-hydrolase, Acylcholine acylhydrolase, atypical cholinesterase, BChE, benzoylcholinesterase, BoBChE, BTCh, BTChI-ChE, BtChoEase, BuChE, butyrocholinesterase, butyryl-ChE, butyrylChE, butyrylcholine esterase, butyrylcholine-hydrolyzing enzyme, butyrylcholinesterase, butyrylcholinesterase K, calcium-activated butyrylcholinesterase, ChE, ChE-II, CholE, choline esterase, choline esterase II (unspecific), cholinesterase, dBChE, DjChE, Djche1, Djche2, EQ-BCHE, eqBChE, EqBuChE, esterase, butyrylcholine, esterase, choline, hBChE, HuBChE, mBuChE I, mBuChE II, monomeric butyrylcholinesterase I, monomeric butyrylcholinesterase II, More, non specific cholinesterase, non-specific cholinesterase, PChE, planarian cholinesterase, plasma cholinesterase, plasma esterase, plasmatic cholinesterase, PoBChE, propionylcholinesterase, pseudo choline esterase, pseudo cholinesterase, pseudocholinesterase, PTChI-ChE, rBChE, serum cholinesterase

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.8 cholinesterase

Purification

Purification on EC 3.1.1.8 - cholinesterase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
6600fold
-
active recombinant enzyme rrBChE from rice cells to 95% purity by tangential flow ultrafiltration, anion exchange chromatography, and Hupresin affinity chromatography
-
ammonium sulfate precipitation and Sephadex G25 gel filtration
-
atypical and typical enzyme
-
monomeric butyrylcholinesterase I and II
-
native enzyme BChE from defatted milk by procainamide affinity chromatography and ultrafiltration, reduced and denatured PoBChE purified by hupresin affinity chromatography
native enzyme BChE from serum by ultrafiltration and immunoaffinity chromatography, recombinant wild-type and mutant enzymes by anion exchange chromatography from CHO cells
native enzyme by a single step procainamide affinity chromatography purification
-
native enzyme from outdated plasma or Cohn Fraction IV-4, large scale, method development, optimization, and evaluation, involving procainamide adsorption chromatography, dialysis, and anion exchange chromatography to 95% purity to homogeneity
-
native enzyme is purified from Cohn fraction IV-4 paste
partial
-
partial, 2 yolk, 2 liver and 1 blood plasma enzyme
-
procainamide gel
-
QFF resin anion-exchange chromatography and Hypatite C column chromatography
-
recombinant C-terminally truncated enzyme BChE from CHO-S cells by affinity chromatography
recombinant enzyme from C57BL/6 mice serum by dialysis, anion exchange chromatography, desalting gel filtration, and procainamide affinity chromatography, followed by ultrafiltration
recombinant extracellular truncated human enzyme from CHO-K1 cell culture medium by Hupresin affinity chromatography, elution is best with 0.1M tetramethylammonium bromide in 20mM TrisCl, pH 7.5, followed by dialysis and ultrafiltration, to homogeneity. Loss of 24% during the dialysis and concentration steps
recombinant full-length enzyme from CHO cells
recombinant human BChE from the milk of transgenic goats to homogeneity
-
recombinant human enzyme from Nicotiana benthamiana by tangential flow ultrafiltration, anion exchange chromatography, and tacrine-huperzine A hybrid (Hupresin) affinity chromatography, method optimization and evaluation, comparison to procainamide affinity chromatography purification method. Citrate buffer at pH 4.0 is selected to minimize extraction of host plant proteins and shows a 4.5fold enhancement in rBChE specific activity compared to Tris buffer, pH 8.0. Anion exchange chromatography increases the purity of rBChE by 70% by removing major host plant protein impurities. The rBChE is then adsorbed to Hupresin® and purified to homogeneity and over 95% purity for an overall process yield of 34%. The purification process represents a 3fold higher product yield over the established process
recombinant wild-type and mutant enzymes from CHO-K1 cells by anion exchange and affinity chromatography
-
separation from acetylcholine esterase
-
VX-inhibited BChE adducts from human plasma by the procainamide affinity gel method or the immunomagnetic separation (IMS) method. The purification efficiency of IMS is 5fold greater than that of the procainamide affinity gel method because the antibody conjugate with protein G magnetic beads ensures highly selective capture and high recovery of VX-inhibited BChE from plasma, overview