نتایج جستجو برای: cholinesterase enzyme inhibitory

تعداد نتایج: 362322  

Journal: :Molecules 2017
Rona R Ramsay Keith F Tipton

The actions of many drugs involve enzyme inhibition. This is exemplified by the inhibitors of monoamine oxidases (MAO) and the cholinsterases (ChE) that have been used for several pharmacological purposes. This review describes key principles and approaches for the reliable determination of enzyme activities and inhibition as well as some of the methods that are in current use for such studies ...

2018
Muhammad Ovais Muhammad Ayaz Ali Talha Khalil Sayed Afzal Shah Muhammad Saeed Jan Abida Raza Muhammad Shahid Zabta Khan Shinwari

BACKGROUND The medicinal importance of a novel plant Olax nana Wall. ex Benth. (family: Olacaceae) was revealed for the first time via HPLC-DAD finger printing, qualitative phytochemical analysis, antioxidant, cholinesterase, and α-glucosidase inhibitory assays. METHODS The crude methanolic extract of O. nana (ON-Cr) was subjected to qualitative phytochemical analysis and HPLC-DAD finger prin...

Journal: :British journal of anaesthesia 1971
J King M J McQueen H G Morgan

By means of dibucaine inhibition (Kalow and Genest, 1957) it was found possible to differentiate three inherited serum cholinesterase phenotypes, those homozygous for the usual enzyme, homozygotes of the atypical enzyme and heterozygous individuals (Kalow and Staron, 1957). Harris and Whittaker (1961) then showed that sodium fluoride could be used to differentiate the serum cholinesterase varia...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 1982
B G Wallace J W Gillon

Acetylcholinesterase (AChE) activity was measured in cholinergic and non-cholinergic neurons in the central nervous system of the leech. Intracellular AChE was assayed by pretreating intact ganglia with echothiophate to inhibit selectively extracellular enzyme. The concentration of intracellular AChE in cholinergic neurons was 3- to 24-fold higher than that in non-cholinergic cells. The propert...

Journal: :Journal of bacteriology 1967
R Marshall L Y Quinn

Type A botulinum toxin was studied for its ability to inhibit the action of acetyl-cholinesterase. The chromogenic substrate, indophenyl acetate, was used for assay of enzyme activity. Inhibition of enzyme function was detected through use of both 6.6 x 10(-6) mg (20 ld(50)) and 6.6 x 10(-10) mg (2 x 10(-3)ld(50)) of type A botulinal toxin. Control assays were performed by use of both homologou...

Journal: :The Biochemical journal 1973
D L Wright D T Plummer

1. Acetylcholinesterase from human erythrocytes was solubilized with Triton X-100 in strong salt solution and partially purified by (NH(4))(2)SO(4) fractionation. This preparation showed three main bands of enzyme activity after electrophoresis on polyacrylamide gel and incubation with either alpha-naphthyl acetate or acetylthiocholine as enzyme substrate. Two of the multiple forms were complet...

Objective(s): Tyrosinase is a key enzyme in pigment synthesis. Overproduction of melanin in parts of the skin results in hyperpigmentation diseases. This enzyme is also responsible for the enzymatic browning in fruits and vegetables. Thus, its inhibitors are of great importance in the medical, cosmetic and agricultural fields. Materials and Methods: A series of twelve kojic acid derivatives wer...

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