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'Acetylcholinesterase' in keywords
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1Author    Dettmar Von WachtendonkRequires cookie*
 Title    in the Haemolymph of the Mussel M ytilus edulis  
 Abstract    A Cholinesterase deriving from the hemolymph of the mussel M ytilus edulis was partially purified by use of gel-permeation and ion-exchange chromatography; the speci-fity to different substrates or inhibitors indicates clearly the occurrence of a "true" acetylcholinesterase. 
  Reference    (Z. Naturforsch. 31c, 333 [1976]; received October 20 1975/February 9 1976) 
  Published    1976 
  Keywords    M ytilu s edulis, Hemolymph, Acetylcholinesterase, Specificity, Inhibition 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0333_n.pdf 
 Identifier    ZNC-1976-31c-0333_n 
 Volume    31 
2Author    K.-P Rueß, M. LiefländerRequires cookie*
 Title    Molecular Forms of Purified Cytoplasmatic and Membrane Bound Bovine-Brain-Acetylcholinesterase Solubilized by Different Methods  
 Abstract    Membrane bound, Triton X-100 solubilized bovine nucleus caudatus acetylcholinesterase is sedimenting in presence of Triton X-100 concentrations higher than the CMC as a 10.5 S-deter-gent-enzyme complex. There is evidence that this complex does neither represent the molecular enzyme arrangement present in the membrane, nor the molecular form originally released from the membrane. The purified, cytoplasmatic acetylcholinesterase is sedimenting as a 10.5 S-form too. This form is clearly to be distinguished from the detergent enzyme complex, for it is obviously not capable of aggregating, whereas the 10.5 S-detergent-enzyme complex aggregates on detergent removal to defined water soluble oligomers with sedimentation coefficients of 16 S (700000 ± 10000), 20.6 S (960000 ± 60000) and 23.3 S (~ 1200000). In contrast to acetylcholinesterase from erythrocytes this aggregation is not easily reversibly by incubation with Triton X-100, reflecting differences in the hydrophobic part o f the enzymes. Purified acetylcholinesterase solubilized without detergent under autolytic or tryptic conditions is mainly sedimenting as a 4.5 S-form. Such slow sedimenting forms detected in crude solubilisates o f neuronal tissues, may originate at least partially form autolytic solubilization. 
  Reference    Z. Naturforsch. 36c, 968—972 (1981); received June 241981 
  Published    1981 
  Keywords    Acetylcholinesterase, Cytoplasmatic, Membrane-Bound, Bovine-Brain, Molecular Forms 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0968.pdf 
 Identifier    ZNC-1981-36c-0968 
 Volume    36 
3Author    Klaus-Dieter Spindler, M. Argarethe Spindler-Barth, Andreas Turberg, G. Ünter, AdamRequires cookie*
 Title    Action of Brassinosteroids on the Epithelial Cell Line from Chironomus tentans  
 Abstract    The two brassinosteroids, 22S',23S'-homobrassinolide and 22S',23S'-homocastasterone are weak com petitors o f the binding o f [3H]ponasterone A to the intracellular ecdysteroid receptor from the epithelial cell line from Chironom us tentans. The relative affinities to the ecdysteroid receptor are 0.001 for both brassinosteroids as compared to 20-OH-ecdysone and 0.1 in com ­ parison to ecdysone. Both substances exert m orphological effects similar to those observed with 20-OH-ecdysone. Like m oulting horm ones both brassinosteroids inhibit chitin synthesis. However, these effects were observed only at rather high concentrations (10-5 to 10"4 m) which were cytotoxic for 22 5,23 S'-homobrassinolide. 
  Reference    Z. Naturforsch. 47c, 280—2 (1992); received October 1/D ecem ber 3 1991 
  Published    1992 
  Keywords    Ecdysteroid Receptor, Acetylcholinesterase, Chitin Synthesis, Brassinosteroids 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0280.pdf 
 Identifier    ZNC-1992-47c-0280 
 Volume    47 
4Author    KunjanR. Dave, AnshuR. Syal, SurendraS. KatyareRequires cookie*
 Title    Tissue Cholinesterases. A Comparative Study of Their Kinetic Properties  
 Abstract    The substrate saturation and temperature-dependent kinetic properties of soluble and membrane-bound forms of acetylcholinestarase (A C h E) from brain and butyrylcholinester­ ase (B C h E) from heart and liver were examined. In simultaneous studies these parameters were also measured for A C h E in erythrocyte membranes and for B C h E in the serum from rat and humans. For both soluble and membrane-bound forms of the enzyme from the three tissues, two components were discernible. In the brain, K m of component I (high affinity) and component II (low affinity) was somewhat higher in membrane-bound form than that of the soluble form components, while the Vmax values were significantly higher by about five fold. In the heart, K m of component II was lower in membrane-bound form than in the soluble form, while Vmax for both the components was about four to six fold higher in the membrane-bound form. In the liver, Vmax was marginally higher for the two components of the membrane-bound enzyme; the K m only of component I was higher by a factor of 2. In the rat erythrocyte membranes three components of A C h E were present showing increasing values of K m and Vmax. In contrast, in the human erythrocyte membranes only two com po­ nents could be detected; the one corresponding to component II of rat erythrocyte mem­ branes was absent. In the rat serum two components of B C h E were present while the human serum was found to possess three components. Component I of the human serum was missing in the rat serum. Temperature kinetics studies revealed that the Arrhenius plots were bi-phasic for most of the systems except for human serum. Membrane binding of the enzyme resulted in decreased energy of activation with shift in phase transition temperature (r t) to near physiological temperature. 
  Reference    Z. Naturforsch. 55c, 100 (2000); received June 16/August 24 1999 
  Published    2000 
  Keywords    Acetylcholinesterase, Butyrylcholinesterase, Substrate Kinetics, Temperature Kinetics 
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 TEI-XML for    default:Reihe_C/55/ZNC-2000-55c-0100.pdf 
 Identifier    ZNC-2000-55c-0100 
 Volume    55 
5Author    H. Großmann, M. W. Einert, M. LiefländerRequires cookie*
 Title    Acetylcholinesterase aus dem Gift von Bungarus multicinctus. Reinigung und Eigenschaften The Acetylcholinesterase of Bungarus multicinctus Venom. Purification and Properties  
 Abstract    Acetylcholinesterase from Banded krait (Bungarus m ulticinctus) venom has been purified by CM -Sephadex chrom atography and affinity chromatography to a specific activity of 4290 U/mg. The purified enzyme is a glycoprotein. It is free of electrophoretically detectable contam inating proteins. A m olecular weight of 140 000 + 5 000 has been determ ined by gradient gel electro­ phoresis for the native enzyme. It is split into two equal-sized subunits (Mr 70 000 + 2 000) by SDS treatm ent. The N -term inal amino acid analysis gave glycine and serine. The purified acetyl­ cholinesterase can be resolved by disc gel electrophoresis into four and by isoelectric focusing into six isozymes. The p i value of the m ain isozyme has been found to be 5.98 + 0.05. 
  Reference    Z. Naturforsch. 34c, 27 (1979); eingegangen am 2. November 1978 
  Published    1979 
  Keywords    Acetylcholinesterase, Snake Venom, B ungarus m ulticinctus, Affinity Chromatography, Isozymes 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0027.pdf 
 Identifier    ZNC-1979-34c-0027 
 Volume    34 
6Author    Stylianos TsakirisRequires cookie*
 Title    Effects of L-Phenylalanine on Acetylcholinesterase, (Na+,K+)-ATPase and Mg2+-ATPase Activities in Adult Rat Whole Brain and Frontal Cortex  
 Abstract    The effect of different L-phenylalanine (Phe) concentrations (0.12-12.1 m M) on acetylcho­ linesterase (AChE), (Na+,K+)-ATPase and Mg2+-ATPase activities was investigated in ho-mogenates of adult rat whole brain and frontal cortex at 37 °C. AChE, (Na+,K+)-ATPase and Mg2+-ATPase activities were determined after preincubation with Phe. AChE activity in both tissues showed a decrease up to 18% (p<0.01) with Phe. Whole brain Na+,K+-ATPase was stimulated by 30-35% (p<0.01) with high Phe concentrations, while frontal cortex Na+,K+-ATPase was stimulated by 50-55% (pcO.OOl). Mg2+-ATPase activity was increased only in frontal cortex with high Phe concentrations. It is suggested that: a) The inhibitory effect of Phe on brain AChE is not influenced by developmental factors, while the stimulation of Phe on brain Na+,K+-ATPase is indeed affected; b) The stimulatory effect of Phe on rat whole brain Na+,K+-ATPase is decreased with age; c) Na+,K+-ATPase is selectively more stimulated by high Phe concentrations in frontal cortex than in whole brain homogenate; d) High (toxic) Phe concentrations can affect Mg2+-ATPase activity in frontal cortex, but not in whole brain, thus modulating the amount of intracellular Mg2+. 
  Reference    Z. Naturforsch. 56c, 132—137 (2001); received September 4/October 4 2000 
  Published    2001 
  Keywords    Acetylcholinesterase, (Na+, K+)-, Mg2 +-ATPase, L-Phenylalanine 
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 TEI-XML for    default:Reihe_C/56/ZNC-2001-56c-0132.pdf 
 Identifier    ZNC-2001-56c-0132 
 Volume    56 
7Author    Stylianos Tsakiris3, Panagiota Kouniniotou-Krontiri3, KleopatraH. Schulpisb, JohnC. Stavridis3Requires cookie*
 Title    L-Phenylalanine Effect on Rat Brain Acetylcholinesterase and Na+,K+-ATPase  
 Abstract    The effect of different L-phenylalanine (Phe) concentrations (0 .1 -1 2 .1 m M) , on acetylcho­ linesterase (A C h E) and N a+,K +-ATPase activities of brain homogenate and pure enzymes, was investigated at 37 °C. A C h E and Na+,K +-ATPase activities were determined according to Ellman G. -6 1 3) respectively, after preincubation with Phe. A C h E activity in brain homogenate or in pure eel E.electricus enzyme showed a decrease, which reached up to 18% with concentrations of 0 .9 -1 2 .1 m M . Brain homogenate N a+,K +-A TPase activity showed an increase 1 6 -6 5 % with 0 .2 4 -0 .9 mM of Phe, while an activity increase of 6 0 -6 5 % appeared with 0 .9 -1 2 .1 mM of Phe. Pure en­ zyme activity (from porcine cerebral cortex) was not affected by high Phe concentrations, while it was increased by low concentrations. The above results suggest: a) A direct effect of Phe on A C h E , b) A direct effect of low Phe concentrations and an indirect effect of high ones on Na+,K +-ATPase. 
  Reference    Z. Naturforsch. 53c, 163 (1998); received September 22/D ecem ber 15 1997 
  Published    1998 
  Keywords    L-Phenylalanine, R at Brain, Acetylcholinesterase, N a+, K +-ATPase, Mg2+-ATPase 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0163.pdf 
 Identifier    ZNC-1998-53c-0163 
 Volume    53 
8Author    Stylianos Tsakiris, Panagoula Angelogianni, JohnC. StavridisRequires cookie*
 Title    Effect of Aging on the Activities of Acetylcholinesterase, Na+, K+-ATPase and Mg2+-ATPase in Rat Pituitary and Hypothalamus  
 Abstract    Acetylcholinesterase (A C h E), N a+, K +-ATPase and Mg2+-A TPase activities were esti­ mated in homogenised rat pituitary and hypothalamus of 4-and 22-month-old rats. A C hE activity was not altered in the pituitary of aged com pared to adult rats, while it was found decreased by about 40% in the hypothalamus. N a+,K +-A TPase activity remained stable in the hypothalamus, while it was decreased by about 38% in the pituitary. Mg2+-A TPase activ­ ity remained unchanged in the hypothalamus, but was increased by about 83% in the pitu­ itary. This pituitary N a+, K +-ATPase inactivation may result in pathological mood and de­ creased neural excitability and metabolic energy production in aged animals.The age-related alterations of A C h E , Na+, K +-ATPase and Mg2+-A TPase activities may reflect changes in secretion and responses of some hormones of pituitary and hypothalamus. 
  Reference    Z. Naturforsch. 53c, 168 (1998); received O ctober 13/O ctober 31 1997 
  Published    1998 
  Keywords    Aging, R at Pituitary, Rat Hypothalamus, Acetylcholinesterase, N a+, K +-ATPase, Mg2+-ATPase 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0168.pdf 
 Identifier    ZNC-1998-53c-0168 
 Volume    53