PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27486373-5 2015 The results revealed that the salt substitutes caused a significant (p<0.05) increase in both AChE and BChE activity and also induced lipid peroxidation in the brain of rats in vivo as well as under in vitro condition in a dose-dependent manner. Salts 30-34 acetylcholinesterase Rattus norvegicus 97-101 3074925-5 1988 The ratio of detergent-soluble AChE to salt-soluble AChE was lower in 30-month-old rats than in 4-month-old rats. Salts 39-43 acetylcholinesterase Rattus norvegicus 52-56 6667556-1 1983 Muscarinic and nicotinic receptor site binding and the activity of choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) in the forebrain and brainstem of Dahl salt-sensitive (DS) and salt-resistant (DR) rats was investigated. Salts 171-175 acetylcholinesterase Rattus norvegicus 104-124 6667556-1 1983 Muscarinic and nicotinic receptor site binding and the activity of choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) in the forebrain and brainstem of Dahl salt-sensitive (DS) and salt-resistant (DR) rats was investigated. Salts 171-175 acetylcholinesterase Rattus norvegicus 126-130 27486373-6 2015 The effect of the salt substitutes on AChE and BChE activities could be attributed to the presence of some toxic heavy metals. Salts 18-22 acetylcholinesterase Rattus norvegicus 38-42 27486373-7 2015 Therefore, the ability of the salt substitutes to induce lipid peroxidation and activate AChE and BChE activities could provide some possible mechanism for their neurotoxic effect. Salts 30-34 acetylcholinesterase Rattus norvegicus 89-93 15882896-1 2005 In the present study, activity of salt soluble (SS) G1 and detergent soluble (DS) G4 molecular isoforms of acetylcholinesterase (AChE) has been investigated in rat brain areas in trained (learned), scopolamine (amnesic) and Tacrine (anti-dementic) treated rats to find out their role in learning and memory functions. Salts 34-38 acetylcholinesterase Rattus norvegicus 107-127 22507914-6 2012 Furthermore, DOCA-salt treatment has shown a significant impairment of vascular endothelial function (DOCA attenuated acetylcholine induced endothelium dependent relaxation), with a significant reduction in serum nitrite/nitrate levels, along with increased aortic, serum and brain oxidative stress levels (aortic superoxide anion, serum and brain thiobarbituric acid reactive species, brain glutathione) and brain acetylcholinesterase activity. Salts 18-22 acetylcholinesterase Rattus norvegicus 415-435 15882896-1 2005 In the present study, activity of salt soluble (SS) G1 and detergent soluble (DS) G4 molecular isoforms of acetylcholinesterase (AChE) has been investigated in rat brain areas in trained (learned), scopolamine (amnesic) and Tacrine (anti-dementic) treated rats to find out their role in learning and memory functions. Salts 34-38 acetylcholinesterase Rattus norvegicus 129-133 12044655-1 2002 Previous studies have shown that an abnormal salt-soluble form of G(1) acetylcholinesterase (AChE) is increased in the Alzheimer"s disease (AD) brain. Salts 45-49 acetylcholinesterase Rattus norvegicus 71-91 12430986-4 2002 Specific activity of acetylcholinesterase was assayed spectrophotometrically in salt-soluble and detergent-soluble fractions of various brain areas: frontal cortex, cerebral cortex, striatum, hippocampus and hypothalamus, thalamus, pons, medulla, and cerebellum. Salts 80-84 acetylcholinesterase Rattus norvegicus 21-41 12044655-1 2002 Previous studies have shown that an abnormal salt-soluble form of G(1) acetylcholinesterase (AChE) is increased in the Alzheimer"s disease (AD) brain. Salts 45-49 acetylcholinesterase Rattus norvegicus 93-97 8360197-4 1993 Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina. Salts 60-64 acetylcholinesterase Rattus norvegicus 22-26 11253171-5 2001 Specific activity (micromoles/min/mg of protein) of AChE was assayed in salt soluble (SS) and detergent soluble (DS) fractions of various brain areas, which consists of predominantly G1 and G4 molecular isoforms of AChE respectively. Salts 72-76 acetylcholinesterase Rattus norvegicus 52-56 8177377-1 1994 Rat brain acetylcholinesterase (AChE, EC 3.1.1.7) consists of about 80% amphiphilic detergent-soluble (DS-) AChE and 20% hydrophilic salt-soluble (SS-) AChE. Salts 133-137 acetylcholinesterase Rattus norvegicus 10-30 8177377-1 1994 Rat brain acetylcholinesterase (AChE, EC 3.1.1.7) consists of about 80% amphiphilic detergent-soluble (DS-) AChE and 20% hydrophilic salt-soluble (SS-) AChE. Salts 133-137 acetylcholinesterase Rattus norvegicus 32-36 8360197-2 1993 High salt and heparin-containing buffers are capable of solubilizing asymmetric AChE molecules from skeletal muscle; however, detachment of AChE specifically from synaptic basal lamina using these procedures has not been demonstrated. Salts 5-9 acetylcholinesterase Rattus norvegicus 80-84 8360197-4 1993 Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina. Salts 60-64 acetylcholinesterase Rattus norvegicus 203-207 8360197-4 1993 Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina. Salts 60-64 acetylcholinesterase Rattus norvegicus 203-207 8360197-4 1993 Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina. Salts 101-105 acetylcholinesterase Rattus norvegicus 203-207 8360197-4 1993 Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina. Salts 101-105 acetylcholinesterase Rattus norvegicus 203-207 1849454-5 1991 The detergent-extracted (DE) 16 S AChE was tightly bound to membranes through detergent-sensitive, high-salt insensitive interactions and was distinct from high-salt-soluble 16 S AChE. Salts 104-108 acetylcholinesterase Rattus norvegicus 34-38 1461372-7 1992 These results are compatible with the existence of a hydrophobic segment present both on salt-soluble and detergent-soluble 11 S AChE as well as on the minor forms 4 S and 7 S. This segment is not linked to the catalytic subunits by disulfide bounds in contrast to the 20 kD non-catalytic subunit described by Inestrosa et al. Salts 89-93 acetylcholinesterase Rattus norvegicus 129-133 1849454-5 1991 The detergent-extracted (DE) 16 S AChE was tightly bound to membranes through detergent-sensitive, high-salt insensitive interactions and was distinct from high-salt-soluble 16 S AChE. Salts 161-165 acetylcholinesterase Rattus norvegicus 34-38 2094823-1 1990 In primary cell cultures of rat superior cervical ganglia (SCG) the tailed asymmetric 16S molecular form of acetylcholinesterase (AChE) possesses hydrophilic (high-salt soluble, HSS) and hydrophobic (detergent extracted, DE) variants. Salts 164-168 acetylcholinesterase Rattus norvegicus 108-128 2094823-1 1990 In primary cell cultures of rat superior cervical ganglia (SCG) the tailed asymmetric 16S molecular form of acetylcholinesterase (AChE) possesses hydrophilic (high-salt soluble, HSS) and hydrophobic (detergent extracted, DE) variants. Salts 164-168 acetylcholinesterase Rattus norvegicus 130-134