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'Photoaffinity Labelling' in keywords
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1990 (1)
1984 (1)
1982 (1)
1Author    Lutz Reum, G. Erd Käuser, U. Lrike Enderle, Jan KoolmanRequires cookie*
 Title    A Steroid-Binding Protein from Insect Haemolymph Isolated by PhotoafTinity Labelling and Immunoadsorption  
 Abstract    Endogenous ecdysteroids as well as radiolabelled exogenous ecdysone were crosslinked to a protein when haemolymph from blowfly larvae was irradiated with UV-light under optimized conditions. This indicates that larval haemolymph of blowflies contains an ecdysteroid-binding protein. The crosslinked ecdysteroid-protein complex was shown to form a ternary complex when mixed with ecdysteroid-specific antibodies. Formation of the ternary complex was due to a specific interaction of the binding sites of the antibodies with the steroid. This specific interaction was used to isolate the ecdysteroid-protein complex from irradiated crude larval haemolymph by immunoadsorption. The method described here represents a rapid approach for the isolation o f steroid-binding proteins by a combination o f photoaffinity labelling and immunoadsorption. 
  Reference    Z. Naturforsch. 37c, 967—9 (1982); received March 11/June 8 1982 
  Published    1982 
  Keywords    Immunoadsorption, Ecdysteroids, Calliphorin, Steroid-Binding Protein, Photoaffinity-Labelling 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0967.pdf 
 Identifier    ZNC-1982-37c-0967 
 Volume    37 
2Author    HelenG M Cfadden, JohnN. PhillipsRequires cookie*
 Title    Synthesis and Use of Radiolabelled Cyanoacrylate Probes of the Photosystem II Herbicide Binding Site  
 Abstract    Cyanoacrylates are potent inhibitors o f photosynthetic electron transport (PET) and are po­ tentially useful probes o f the photosystem II herbicide binding site. A series o f cyanoacrylates was synthesized and the Hill inhibition activities evaluated in order to select com pounds suita­ ble for radioactive synthesis. A cyanoacrylate, 2-(2-nitrophenoxy)ethyl 3-benzylamino-2-cyano-2-pentenoate, was found to displace diuron from the photosystem II herbicide binding site. For this compound the dissociation constant o f the inhibitor/binding site complex was found to be 2 x 10"8 M with an active site concentration o f 2 nm ol/m g chlorophyll. In a similar system the corresponding figures for diuron were 1.2 x 10"8 m and 1.3 nm ol/m g chlorophyll. Photoaffinity labelling o f 1% II thylakoid proteins with 2-(2-azidophenoxy)ethyl 3-[7-l4C]-benzylam ino-2-cyano-2-pentenoate showed weak binding in the 32 and 28 kD mass regions, consistent with binding to the D, peptide. 
  Reference    Z. Naturforsch. 45c, 196—202 (1990); received September 20/N ovem ber 10 1989 
  Published    1990 
  Keywords    Cyanoacrylate, Photoaffinity Labelling, Photosystem II, Com petitive Inhibition, Diuron 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0196.pdf 
 Identifier    ZNC-1990-45c-0196 
 Volume    45 
3Author    Hans-Peter Stupp, MartinG. PeterRequires cookie*
 Title    Juvenile Hormone III as a Natural Ligand for Photoaffinity Labelling of JH-Binding Proteins  
 Abstract    Juvenile hormone III, i.e. methyl 10,1 l-epoxy-3,7-dimethyl-2£',6£'-dodecadienoate, was used for photoaffinity labelling of JH-binding proteins. Irradiation of haemolymph from Manduca sexta and Locusta migratoria in the presence of racemic [10-3H]JH-III results in covalent 
  Reference    Z. Naturforsch. 39c, 1145—1149 (1984); received April 26/July 23 1984 
  Published    1984 
  Keywords    Insect Haemolymph, Hormone Binding Proteins, Juvenile Hormone, Photoaffinity Labelling, Manduca sexta, Locusta migratoria 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1145.pdf 
 Identifier    ZNC-1984-39c-1145 
 Volume    39