Feasibility of Acetylcholinesterase Reaction Assay Monitoring in DIUTHAME-MS

2020 ◽  
Vol 31 (10) ◽  
pp. 2154-2160
Author(s):  
Yasuhide Naito ◽  
Masahiro Kotani ◽  
Takayuki Ohmura
Keyword(s):  
Acetylcholinesterase Reaction

scholarly journals Finite Element Analysis of the Time-Dependent Smoluchowski Equation for Acetylcholinesterase Reaction Rate Calculations

2007 ◽  
Vol 92 (10) ◽  
pp. 3397-3406 ◽  
Author(s):  
Yuhui Cheng ◽  
Jason K. Suen ◽  
Deqiang Zhang ◽  
Stephen D. Bond ◽  
Yongjie Zhang ◽  
...  
Keyword(s):  
Finite Element Analysis ◽  
Finite Element ◽  
Reaction Rate ◽  
Smoluchowski Equation ◽  
Time Dependent ◽  
Element Analysis ◽  
Acetylcholinesterase Reaction

A sensitive biosensor for the fluorescence detection of the acetylcholinesterase reaction system based on carbon dots

2015 ◽  
Vol 125 ◽  
pp. 90-95 ◽  
Author(s):  
Xiangling Ren ◽  
Jianfei Wei ◽  
Jun Ren ◽  
Li Qiang ◽  
Fangqiong Tang ◽  
...  
Keyword(s):  
Fluorescence Detection ◽  
Carbon Dots ◽  
Reaction System ◽  
Acetylcholinesterase Reaction

Microphotometric dynamic analysis of the histochemical acetylcholinesterase reaction

2007 ◽  
Vol 82 (6) ◽  
pp. 311-317
Author(s):  
A Yu Budantsev ◽  
Ov Kornilova ◽  
Bi Medvedev
Keyword(s):  
Dynamic Analysis ◽  
Acetylcholinesterase Reaction

Ultrastructural Cytochemistry of Acetylcholinesterase Enzyme Activity in Pancreatic Tissue Transplants in Rats

1994 ◽  
Vol 3 (2) ◽  
pp. 171-177 ◽  
Author(s):  
Ernest Adeghate ◽  
Tibor Donáth
Keyword(s):  
Enzyme Activity ◽  
Enzyme Reaction ◽  
Ultrastructural Level ◽  
Pancreatic Tissue ◽  
Reaction Products ◽  
Nerve Fibres ◽  
Tissue Transplants ◽  
Acetylcholinesterase Reaction ◽  
Acetylcholinesterase Enzyme ◽  
Product Forms

The distribution of acetylcholinesterase (AChE) at the ultrastructural level was investigated in normal and in pancreatic fragments transplanted for 56 days into the anterior eye chamber of heterologous rats using enzyme cytochemical methods. Acetylcholinesterase reaction products were seen on the basal surface of the acinar cells in normal pancreas. Acetylcholinesterase enzyme activity was also detected on the axolemma of the surviving nerve fibres. This enzyme reaction product forms alternating thick and thin bands on the axolemma. Some of these AChE-positive nerve fibres accompany blood vessels that also survive after transplantation. AChE were seen in cytoplasm adjacent to the surviving alpha and pancreatic polypeptide cells. We conclude that the ability of some neurons and cells to produce and or store acetylcholinesterase is still retained after transplantation of pancreatic tissue into the anterior eye chamber of rats.

scholarly journals Specific localization of the alpha-latrotoxin receptor in the nerve terminal plasma membrane.

1984 ◽  
Vol 99 (1) ◽  
pp. 124-132 ◽  
Author(s):  
F Valtorta ◽  
L Madeddu ◽  
J Meldolesi ◽  
B Ceccarelli
Keyword(s):  
Plasma Membrane ◽  
Nerve Terminal ◽  
Neuromuscular Junctions ◽  
Proteolytic Enzymes ◽  
Dry Weight ◽  
Major Protein ◽  
Frog Neuromuscular Junction ◽  
Acetylcholinesterase Reaction ◽  
Specific Localization ◽  
The One

The receptor for alpha-latrotoxin, the major protein component of the black widow spider venom, was investigated by the use of the purified toxin and of polyclonal, monospecific anti-alpha-latrotoxin antibodies. Experiments on rat brain synaptosomes (where the existence of alpha-latrotoxin receptors was known from previous studies) demonstrated that the toxin-receptor complex is made stable by glutaraldehyde fixation. At saturation, each such complex was found to bind on the average five antitoxin antibody molecules. In frog cutaneous pectoris muscles, the existence of a finite number of high-affinity receptors was revealed by binding experiments with 125I-alpha-latrotoxin (Kd = 5 X 10(-10) M; bmax = 1.36 +/- 0.16 [SE] X 10(9) sites/mg tissue, dry weight). Nonpermeabilized muscles were first treated with alpha-latrotoxin, and then washed, fixed, dissociated into individual fibers, and treated with anti-alpha-latrotoxin antibodies and finally with rhodamine-conjugated sheep anti-rabbit antibodies. In these preparations, muscle fibers and unmyelinated preterminal nerve branches were consistently negative, whereas bright specific fluorescent images, indicative of concentrated alpha-latrotoxin binding sites, appeared in the junctional region. These images closely correspond in size, shape, and localization to endplates decorated by the acetylcholinesterase reaction. The presynaptic localization of the specific fluorescence found at frog neuromuscular junctions is supported by two sets of findings: (a) fluorescent endplate images were not seen in muscles that had been denervated; and (b) the distribution of fluorescence in many fibers treated with alpha-latrotoxin at room temperature was the one expected from swollen terminal branches. Swelling of terminals is a known morphological change induced by alpha-latrotoxin in this preparation. When muscles were treated with either proteolytic enzymes (trypsin, collagenase) or detergents (Triton X-100) before exposure to alpha-latrotoxin, the specific fluorescent endplate images failed to appear. Taken together these findings indicate that the alpha-latrotoxin receptor is an externally exposed protein highly concentrated in the nerve terminal plasma membrane. Its density (number per unit area) at the frog neuromuscular junction can be calculated to be approximately 2,400/micron2.

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