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1979 (1)
1Author    G. Erhild, N. Urm, Ann, D. Ieter StrackRequires cookie*
 Title    Sinapine Esterase I. Characterization of Sinapine Esterase from Cotyledons of Raphanus sativus  
 Abstract    From cotyledons o f Raphanus sativus (red radish) an esterase activity which catalyzes the hy­ drolysis o f sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optim um o f 8.5 and the apparent K m is 1.95 x 10~5 m. The enzyme is relatively insensi­ tive to both physostigm ine (eserine) {K x = 1.73 x 10-4 m) and neostigm ine (A'i = 2 .1 3 x 10-4 m). Diisopropyl fluorophosphate (D F P) showed no inhibition and diethyl /?-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10-5 m, respectively. Choline (10~2 m) was inhibitory but acetylcholine (1 0 -2 m) stimulated the enzyme activity. 
  Reference    Z. Naturforsch. 34c, 715—720 (1979); received June 11 1979 
  Published    1979 
  Keywords    Esterase, Sinapine, Sinapic Acid Esters, Raphanus, Brassicaceae, High-Performance Liquid Chro­ matography (HPLC) 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0715.pdf 
 Identifier    ZNC-1979-34c-0715 
 Volume    34