About: Affinity chromatography of acetylcholinesterase

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scientific article published on 01 January 1974

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1974 (uk) articolo scientifico (pubblicato il 1974) (it) article scientifique publié en 1974 (fr) im Januar 1974 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 1974 (ast) artikull shkencor i botuar më 01 janar 1974 (sq) scientific article published on 01 January 1974 (en)
publication date	wds:Q68872819-EC9B39B2-6140-40DA-A7DF-554C91CBA9A9
publication date	1974-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68872819-F0B63A3A-6EA9-436F-9B46-901075B368AA
language of work or name	English
cites work	wds:Q68872819-34326FEB-9D48-434A-9BA9-3985F725ED47 wds:Q68872819-35CA571D-F8B9-4809-935B-15C0EA25ED1F wds:Q68872819-3656C7E5-A0E0-4BF1-92C7-4EA944126FAE wds:Q68872819-36757302-5534-464B-A180-B15D635B1B6F wds:Q68872819-983C5309-F843-4B18-8B04-693B076BACDD wds:Q68872819-B451A7BA-C45B-4C19-9F94-09B05B5B86E1 wds:Q68872819-B5B32EF5-00E1-4193-A707-2FFFAB361340 wds:Q68872819-B6571080-2A13-4F03-AA3B-6334164CD8CE wds:Q68872819-BBAE2EAC-4D8B-4616-B233-EF472FE97AE8 wds:Q68872819-C4F33B95-B005-4A6B-9A58-85611B2C1C4A wds:Q68872819-E2186759-22C4-4BA1-AC1E-98478136469A wds:Q68872819-FB75A446-72DE-4A2E-A40F-65E13F3E91B4
cites work	Chemical Coupling of Peptides and Proteins to Polysaccharides by Means of Cyanogen Halides The Purification of Papain by Affinity Chromatography [Solubilization of electric organ acetylcholinesterase from eels. Action of trypsin] Enzyme regulation in neuroblastoma cells. Selection of clones with low acetylcholinesterase activity and the independent control of acetylcholinesterase and choline-O-acetyltransferase Proteins in excitable membranes: their properties and function in bioelectricity are discussed [Acetylcholinesterase of fish electric organs (torpedo and electric eel); membrane complexes] Purification by affinity chromatography of acetylcholinesterase from electric organ tissue of the electric eel subsequent to tryptic treatment A PARTIAL CHARACTERIZATION OF ACETYLCHOLINESTERASE Fluorescent probes of acetylcholinesterase A method for the purification of acetylcholinesterase by affinity chromatography Purifcation and properties of multiple forms of brain acetylcholinesterase (EC 3.1.1.7) A covalent affinity column for the purification of acetylcholinesterase
author name string	wds:Q68872819-E36D0E49-554C-4A83-A7AF-E9FB5DCE0668
author name string	I Silman
rdfs:label	Affinity chromatography of acetylcholinesterase (en) Affinity chromatography of acetylcholinesterase (nl) Affinity chromatography of acetylcholinesterase (sq)
skos:prefLabel	Affinity chromatography of acetylcholinesterase (en) Affinity chromatography of acetylcholinesterase (nl) Affinity chromatography of acetylcholinesterase (sq)
name	Affinity chromatography of acetylcholinesterase (en) Affinity chromatography of acetylcholinesterase (nl) Affinity chromatography of acetylcholinesterase (sq)
author	wds:Q68872819-5AA45924-F2C0-45D1-B698-F90D37992B37
author	Yadin Dudai
title	wds:Q68872819-0901D322-EE35-498D-BF8E-38562141EA85
title	Affinity chromatography of acetylcholinesterase (en)
page(s)	wds:Q68872819-DAC8AD56-D193-4977-B335-BD23BC0A64C2
page(s)	571-580
instance of	wds:Q68872819-E60A1934-3E2C-4597-A7AC-37512D7FEFAC
instance of	scholarly article
PubMed ID	wds:Q68872819-11621285-6E26-4A03-80A4-EF802A8A411A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4449474
PubMed ID	4449474
published in	wds:Q68872819-9EECA3BC-7AFF-42DA-9FFD-3C8CE7865289
published in	Methods in Enzymology
volume	wds:Q68872819-49844455-E753-4DBC-AEC0-B22B08E9E80E
volume	34
DOI	wds:Q68872819-7B34712C-1E59-47D2-90B8-254A2F2FD79A
DOI	http://dx.doi.org/10.1016/S0076-6879(74)34076-1
DOI	10.1016/S0076-6879(74)34076-1
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68872819
is cites work of	Molecular structure of elongated forms of electric eel acetylcholinesterase The Dependence of Acetylcholinesterase Aggregation at Low Ionic Strength upon a Polyanionic Component An Immunological Study of Rat Acetylcholinesterase: Comparison with Acetylcholinesterases from Other Vertebrates Use of procainamide gels in the purification of human and horse serum cholinesterases Electrophorus electricus as a model system for the study of membrane excitability Existence of an inactive pool of acetylcholinesterase in chicken brain Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase Detection of hydroxyproline in preparations of acetylcholinesterase from the electric organ of the electric eel The induction by protons of ion channels through lipid bilayer membranes Immunological Cross-Reactivity between Electric-Eel Acetylcholinesterase and Rat-Tail-Tendon Collagen Partial purification and some properties of a cholinesterase from bush bean (Phaseolus vulgaris L.) roots Acetylcholinesterase of Schistosoma mansoni--functional correlates. Contributed in honor of Professor Hans Neurath's 90th birthday Comparison of low- and high-pressure affinity chromatography for the purification of serine and sulfhydryl esterases Purification and properties of monomeric (G1) forms of acetylcholinesterase secreted by Nippostrongylus brasiliensis The interaction of purified acetylcholinesterase from pig brain with liposomes Proton-induced ion channels through lipid bilayer membranes Characterization of membranes obtained from electric organ of the electric eel by sucrose gradient fractionation and by microdissection Comparative affinity chromatography of acetylcholinesterases from five vertebrate species On the homogeneity of 11-S acetylcholinesterase Affinity chromatography of acetylcholinesterase from Electrophorus electricus electroplax. Investigations on 9-aminoalkylacridine affinity ligands [Synthesis of N-methylacridinium-Sepharose: its utilization in the purification of cholinesterases] Purification of acetylcholinesterase from pig cerebral cortex by affinity chromatography Affinity chromatography of acetylcholinesterase. The use of Amberlite CG-120 for dissociating the enzyme-inhibitor complex Kinetic and structural relationships of transition monomeric and oligomeric carboxyl‐ and choline‐esterases
is cites work of	wds:Q41554365-A44FF1AF-1CFE-453D-913E-D98B30A4266E wds:Q42936100-F85FFC2D-0980-4C68-A6EB-D12264EBCEC3 wds:Q70766930-2436B371-E663-4A8A-8208-64B39E7F34B0 wds:Q39825201-36BBC87E-8300-44E2-BC83-FD5608527F68 wds:Q45162486-A72A9664-8C17-47EB-B61A-3C1F399BC45E wds:Q74225213-007347AC-321E-422E-B582-97C89D314F6C wds:Q34186720-4CA6D159-1E7F-4258-9E61-3FD1EBF9989B wds:Q41043426-E17B16FE-6966-4EE1-92C1-5D83FD5802E0 wds:Q44836044-A9B3D817-C322-4DE7-A094-5469D883C13F

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