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1986 (1)
1975 (1)
1Author    Martin Bopp, Werner LüdickeRequires cookie*
 Title    Über den Abbau des Sinapins während der frühen Ontogenese der Keimlinge von Sinapis alba L. Degradation of Sinapine during the Early Development of Sinapis alba L  
 Abstract    The amount of sinapine in immature seeds of Sinapis alba is very low; it increases during ripening. Most of the sinapine is located in the cotyledons. Hypocotyls and roots contain only traces of it. During the early development of seedlings the amount of sinapine in the cotyledons decreases in 26 °C very rapidly. Simultaneously the amount of a substance X increases. Darkness retarded both these processes. The same effect has a temperature of 10 °C. In both cases the increase of X is completly proportional to the decrease of sinapine. Therefore X is probably a derivative of sinapine. After pretreatment with 26 C amount of sinapic acid increases only in the at a very low level for a long period. 
  Reference    (Z. Naturforsch. 30c, 663 [1975]; eingegangen am 12. Mai 1975) 
  Published    1975 
  Keywords    Sinapis alba, Sinapine, Sinapic Acid, Seedling Development 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0663.pdf 
 Identifier    ZNC-1975-30c-0663 
 Volume    30 
2Author    Remigius Manderscheid, Aloysius WildRequires cookie*
 Title    Characterization of Glutamine Synthetase of Roots, Etiolated Cotyledons and Green Leaves from Sinapis alba (L.)  
 Abstract    Glutamine synthetase of roots, etiolated cotyledons and green leaves from mustard plants cannot all clearly be separated by DEAE-Sephacel chromatography. However, the enzyme of the roots, etiolated cotyledons and green leaves, respectively, differed in the kinetic properties deter­ mined in the crude extract. The root enzyme showed a pH-optimum of about 6.9, a K m value of 3 m M for glutamate and a temperature optimum at 48 °C. Glutamine synthetase of etiolated cotyledons possessed a Km for glutamate of 6 or 12 m M , depending on the dithioerythritol con­ centration in the homogenisation buffer and a temperature optimum at 46 °C. The enzyme of green leaves was characterized by a temperature optimum at 40 °C, a pH-optimum at about 7.4 and a low glutamate affinity with positive cooperative substrate binding. Based on isolation of chloroplasts and identification of glutamine synthetase the enzyme of green leaves seems to be the chloroplastic form. This enzyme was purified by DEAE-Sephacel, hydroxylapatite and Sephacryl S-300 chromatography. Affinity for glutamate and M g S04 of the purified enzyme differed from that found in the crude extract. The function of the different isoenzymes is discussed. Intro du ction 
  Reference    Z. Naturforsch. 41c, 712 (1986); received March 17 1986 
  Published    1986 
  Keywords    Enzyme Purification, Glutamine Synthetase, Isoenzymes, Photorespiration, Sinapis alba 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0712.pdf 
 Identifier    ZNC-1986-41c-0712 
 Volume    41