PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8306998-9 1994 In low-salt-soluble and high-salt-soluble extracts, AChE was solubilised as a hydrophilic globular form, probably a dimeric G2. Salts 29-33 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 12044655-6 2002 However, analysis of salt-extractable AChE isoforms revealed an increase in the proportion of G(1) in both cortex and CSF, similar to that previously observed in AD patients. Salts 21-25 acetylcholinesterase (Cartwright blood group) Homo sapiens 38-42 10585885-5 1999 The bound acetylcholinesterase could be progressively eluted by increasing the salt concentration, with approx. Salts 79-83 acetylcholinesterase (Cartwright blood group) Homo sapiens 10-30 11341928-0 2001 Comparison of salt effects on the reactions of acetylcholinesterase with cationic and anionic inhibitors. Salts 14-18 acetylcholinesterase (Cartwright blood group) Homo sapiens 47-67 11341928-3 2001 In contrast to the salt effects on the reaction of acetylcholinesterase with cationic compounds, it does not include contribution from the enzyme charges. Salts 19-23 acetylcholinesterase (Cartwright blood group) Homo sapiens 51-71 9367582-5 1997 The long-term stability of acetylcholinesterase at the air/water interface was demonstrated for pH 6.5 and a salt concentration of 10(-2) M (KCl). Salts 109-113 acetylcholinesterase (Cartwright blood group) Homo sapiens 27-47 8306998-5 1994 97% of AChE was extractable in low-salt and high-salt detergent-free buffers, and only 3% was solubilised by a further extraction in the presence of Triton X-100. Salts 35-39 acetylcholinesterase (Cartwright blood group) Homo sapiens 7-11 8306998-5 1994 97% of AChE was extractable in low-salt and high-salt detergent-free buffers, and only 3% was solubilised by a further extraction in the presence of Triton X-100. Salts 49-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 7-11 8306998-7 1994 Sucrose density centrifugation revealed that AChE in all somatic extracts (low-salt, high-salt and detergent) resolved almost exclusively as a single peak between 6.9-7.5 S, while excretory/secretory products resolved at 8.2 S. These values are all compatible with dimers of catalytic subunits and no evidence was found for the presence of higher oligomers such as asymmetric forms. Salts 79-83 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-49 8306998-7 1994 Sucrose density centrifugation revealed that AChE in all somatic extracts (low-salt, high-salt and detergent) resolved almost exclusively as a single peak between 6.9-7.5 S, while excretory/secretory products resolved at 8.2 S. These values are all compatible with dimers of catalytic subunits and no evidence was found for the presence of higher oligomers such as asymmetric forms. Salts 90-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-49 8306998-9 1994 In low-salt-soluble and high-salt-soluble extracts, AChE was solubilised as a hydrophilic globular form, probably a dimeric G2. Salts 7-11 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 20501161-6 1987 We describe here at least two distinct AChE pools, according to their differential solubility in non-ionic detergent and high-salt media. Salts 126-130 acetylcholinesterase (Cartwright blood group) Homo sapiens 39-43 20501292-2 1988 In the (C) fraction, tailed asymmetric 16S AChE required high salt conditions to be extracted, while in (A) and (S) microsomal membranes, a collagenase sensitive 16S form, was extracted by detergent alone. Salts 62-66 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-47 3691807-1 1987 It is shown that the salt effect in acetylcholinesterase-catalyzed hydrolysis of 2-(N-methylmorpholinium)-ethylacetate can be quantitatively described by the equation log(k2/KS) = log(k2/KS) degrees--psi log[M+Z] following from Manning"s polyelectrolyte theory; the psi values for salts with univalent and bivalent cations at different pH values of the reaction medium were in accordance with the conclusions of the theory. Salts 21-25 acetylcholinesterase (Cartwright blood group) Homo sapiens 36-56 8360678-1 1993 Cercopithecus monkey brain acetylcholinesterase (AChE; EC 3.1.1.7) consists of about 15% hydrophilic, salt-soluble enzyme and 83% amphiphilic, detergent-soluble enzyme. Salts 102-106 acetylcholinesterase (Cartwright blood group) Homo sapiens 27-47 8360678-1 1993 Cercopithecus monkey brain acetylcholinesterase (AChE; EC 3.1.1.7) consists of about 15% hydrophilic, salt-soluble enzyme and 83% amphiphilic, detergent-soluble enzyme. Salts 102-106 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-53 8360678-2 1993 Sucrose density gradient centrifugation showed that hydrophilic, salt-soluble AChE was composed of about 85% tetramer (10.3S) and 15% monomer (3.3S). Salts 65-69 acetylcholinesterase (Cartwright blood group) Homo sapiens 78-82 8099499-5 1993 The data show that the influence of salts on the electrostatic contribution to the energy of binding of cationic substrates and inhibitors by acetylcholinesterase can be quantitatively described proceeding from the counterion condensation model of Manning by using only one empirical parameter psi+1 for a given subtype or modified form of the enzyme. Salts 36-41 acetylcholinesterase (Cartwright blood group) Homo sapiens 142-162 3973587-0 1985 Molecular forms of acetylcholinesterase from human caudate nucleus: comparison of salt-soluble and detergent-soluble tetrameric enzyme species. Salts 82-86 acetylcholinesterase (Cartwright blood group) Homo sapiens 19-39 3973587-3 1985 The purified, tetrameric salt-soluble (SS) AChE sedimented at 10.6 S and did not bind detergents. Salts 25-29 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-47 30463700-4 2019 These two factors i.e. high salt concentration in the bulk medium and less viscous membranes, allow a deeper insertion of the EGCG into the lipid bilayer, thus leading to a greater inhibition of AChE. Salts 28-32 acetylcholinesterase (Cartwright blood group) Homo sapiens 195-199 2861006-1 1985 In the caudate nucleus of the species tested about 20% of the acetylcholinesterase was salt soluble and sedimented in sucrose density gradient centrifugation as monomeric 5 S and tetrameric 10 S enzyme. Salts 87-91 acetylcholinesterase (Cartwright blood group) Homo sapiens 62-82 736567-0 1978 Acetylcholinesterase: differential affinity chromatographic purification of 11 S and 18 S plus 14 S forms; the importance of multiple-site interactions and salt concentration. Salts 156-160 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 6743696-1 1984 Two soluble forms of AChE from lymphocyte membrane have been obtained, the Triton solubilized Sd form and the high molar salt solubilized Ss form. Salts 121-125 acetylcholinesterase (Cartwright blood group) Homo sapiens 21-25 4733238-2 1973 Acetylcholinesterase from human erythrocytes was solubilized with Triton X-100 in strong salt solution and partially purified by (NH(4))(2)SO(4) fractionation. Salts 89-93 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 21838142-3 2011 Results show harmine in form of base and salt in water and in mixture of DMSO and water has the hightest inhibition activity on ACHE using eserine as reference substance. Salts 41-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 29773682-2 2018 To investigate oximate water structure changes in this reaction, reactivation of paraoxon-inhibited human acetylcholinesterase (AChE) was performed by the oxime asoxime (HI-6) at different pH in the presence and absence of lyotropic salts: a neutral salt (NaCl), a strong chaotropic salt (LiSCN) and strong kosmotropic salts (ammonium sulphate and phosphate HPO42-). Salts 233-237 acetylcholinesterase (Cartwright blood group) Homo sapiens 106-126 29773682-2 2018 To investigate oximate water structure changes in this reaction, reactivation of paraoxon-inhibited human acetylcholinesterase (AChE) was performed by the oxime asoxime (HI-6) at different pH in the presence and absence of lyotropic salts: a neutral salt (NaCl), a strong chaotropic salt (LiSCN) and strong kosmotropic salts (ammonium sulphate and phosphate HPO42-). Salts 233-237 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 29773682-2 2018 To investigate oximate water structure changes in this reaction, reactivation of paraoxon-inhibited human acetylcholinesterase (AChE) was performed by the oxime asoxime (HI-6) at different pH in the presence and absence of lyotropic salts: a neutral salt (NaCl), a strong chaotropic salt (LiSCN) and strong kosmotropic salts (ammonium sulphate and phosphate HPO42-). Salts 250-254 acetylcholinesterase (Cartwright blood group) Homo sapiens 106-126 29773682-2 2018 To investigate oximate water structure changes in this reaction, reactivation of paraoxon-inhibited human acetylcholinesterase (AChE) was performed by the oxime asoxime (HI-6) at different pH in the presence and absence of lyotropic salts: a neutral salt (NaCl), a strong chaotropic salt (LiSCN) and strong kosmotropic salts (ammonium sulphate and phosphate HPO42-). Salts 250-254 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 29773682-4 2018 Reactivation kinetics showed that the low concentration of chaotropic salt up to 75 mM increased the percentage of reactivation of diethylphosphorylated AChE whereas kosmotropic salts lead only to a small decrease in reactivation. Salts 70-74 acetylcholinesterase (Cartwright blood group) Homo sapiens 153-157