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1979 (2)
1974 (1)
1Author    Frank Seela, Wolfgang WesemannRequires cookie*
 Title    Trägergebundene Serotoninderivate und Affinitätschromatographie synaptischer Membranproteine Resin Linked Derivatives of Serotonin and Affinity Chromatography of Proteins Isolated from Synaptic Membranes  
 Abstract    An affinity resin for the isolation of the serotonin receptor from nerve ending membranes was prepared by coupling tryptamine, 5-methoxy-tryptamine or serotonin to CNBr-activated Sepharose 4 B. The tryptamine derivatives, N-6-(aminohexyl)-tryptamines, were obtained by subsequent con­ densation of the corresponding indole derivatives with oxalyl chloride and t-aminocaproamide and reduction with L iA lH 4 . The 6-aminohexyl-group was used as spacer to link covalently the primary amino-group of tryptamine to agarose. — An extract of membrane proteins isolated from rat brain was resolved on this affinity resin into two fractions as compared with only one fraction using unsubstituted Sepharose 4 B. 
  Reference    (Z. Naturforsch. 29c, 248—256 [1974]; eingegangen am 2. Januar/15. Februar 1974) 
  Published    1974 
  Keywords    Affinity Chromatography, Receptor, Resin Linked Serotonin, Synaptic Membrane Proteins 
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 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0248.pdf 
 Identifier    ZNC-1974-29c-0248 
 Volume    29 
2Author    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 
3Author    SatishK. Sharma, JinnieM. Garrett, StewartA. BrownRequires cookie*
 Title    Separation of the S-Adenosylmethionine: 5-and 8-Hydroxyfuranocoumarin O-Methyltransferases of Ruta graveolens L. by General Ligand Affinity Chromatography  
 Abstract    Two S-adenosyl-L-methionine:furanocoumarin O-methyltransferases of R . graveolens, acting at the 5-and 8-hydroxyls of the psoralen nucleus, were completely resolved by adsorption on a general affinity ligand, 5 -(3-carboxypropanamido) xanthotoxin, followed by specific desorption by bergaptol and xanthotoxol, respectively. The 5-O-methyltransferase was purified 450-fold by this procedure, the 8-O-methyltransferase 112-fold, and both enzyme fractions were electrophoretically homogeneous. No resolution could be achieved of the activity against two 5-hydroxypsoralens or of the activity against two 8-hydroxypsoralens, and conclusive evidence is presented for the existence of only one 5-O-methyltransferase and only one 8-O-methyltransferase acting on linear furanocoumarins. In tro d u c tio n 
  Reference    Z. Naturforsch. 34c, 387 (1979); received March 9 1979 
  Published    1979 
  Keywords    Coumarins, Furanocoumarins, O-Methyltransferases, Affinity Chromatography, R u ta graveolens 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0387.pdf 
 Identifier    ZNC-1979-34c-0387 
 Volume    34