Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Additionally we are shipping Butyrylcholinesterase Antibodies (117) and Butyrylcholinesterase Kits (18) and many more products for this protein.
Showing 10 out of 20 products:
the molecular mechanisms by which point mutations may lead to silent BChE variant or alter catalytic activity, is reported.
BChE expression might be regulated by alpha-linolenic acid in HepG2 cells.
Nine out of 18 (50%) individuals with butyrylcholinesterase activity below 2000 U/L had a mutation in 5'UTR (32G/A), intron 2 (c.1518-121T/C) or exon 4 (c.1699G/A; the K variant mutation).
No significant difference in BChE levels of healthy pregnant women and high-risk pregnant women who had undergone a cesarean section under general anesthesia.
Association between polymorphisms of BCHE and vitiligo (show MITF Proteins) in a two-step genetic association study. Upon confirmation of genetic association, the effect was investigated by a genotype-phenotype correlation experiment.
Low serum Butyrylcholinesterase levels are associated with recurrence in prostate cancer.
BCHE-K is associated with a reduced risk for Alzheimer disease and Lewy body dementia whereas APOEvarepsilon4 is associated with more rapid cognitive decline.
Low BChE activity as a predictor of mortality in acute myocardial infarction might be related to its association with poor cardiac function.
rs1803274 polymorphism of the BCHE gene represents a risk factor for in-stent restenosis after percutaneous coronary intervention.
Complement component C3 and butyrylcholinesterase activity are associated with neurodegeneration and clinical disability in multiple sclerosis.
The structure of bovine pancreatic RNase A (show RNASE1 Proteins) has been determined in complex with 2'-deoxyguanosine-5'-monophosphateat 1.33 A resolution.
the absence of BChE leads to diminished fibrillar Abeta (show APP Proteins) deposition in amygdala, hippocampal formation, thalamus and basal ganglia.
It was concluded that in adult murine bone the role of BChE is limited to bone specific changes in microarchitecture and to an increase in relative number of bone resorbing osteoclasts.
Mice that had undergone gene transfer with mouse CocH (show COCH Proteins) (mCocH) showed no place preference or aversion after repeated treatments with a near-lethal 80 mg/kg cocaine dose.
we conclude that toxoplasmosis reduces BChE activity in mice, and this alteration is probably related to the liver damage caused by the parasitism
For metacarb and isocarb, inhibition of BChE w.t. was 260 and 35 times, respectively, faster than inhibition of AChE w.t. For four mutants inhibition was faster than for AChE w.t. but none reached the inhibition rate of BChE.
The localization of BChE in the secondary folds of the neuromuscular junction suggests that this enzyme is not a strict surrogate of AChE and that the two enzymes have two different roles.
The effects of porphyrinogenic drugs on the brain cholinergic system (Ache, Bche, and Chrm1 (show CHRM1 Proteins) levels in various regions of the brain) were examined to establish a mechanism for neurological syndrome displayed in acute porphyrias.
A possible mechanism for partial compensation of tetanic fade in acetylcholinesterase (show AChE Proteins) knockout mice is hydrolysis of acetylcholine by normal levels of endogenous butyrylcholinesterase.
The BChE knockout mouse will allow us to test the hypothesis that the function of BChE is to detoxify poisons and will allow testing the role of BChE in other physiological functions.
These findings show that BCHE can hydrolyze 2-Arachidonoylglycerol which may be evidence of a more specific role for BCHE in endocannabinoid regulation.
Data indicate that polyproline peptides of various lengths and sequences are included in the tetramer structure of butyrylcholinesterase, and the function of these polyproline peptides is to serve as tetramer-organizing peptides.
proline-rich peptides organize the 4 subunits of BChE into a 340 kDa tetramer, by interacting with the C-terminal BChE tetramerization domain
Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage.
, acylcholine acylhydrolase
, butyrylcholine esterase
, choline esterase II
, cholinesterase (serum) 2
, cholinesterase 1