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1978 (1)
1Author    VickiD. Breazeale, BobB. Buchanan, RicardoA. WolosiukRequires cookie*
 Title    Chloroplast Sedoheptulose 1,7-Bisphosphatase: Evidence for Regulation by the Ferredoxin/Thioredoxin System  
 Abstract    1. A substrate-specific sedoheptulose-l,7-bisphosphatase has been found in chloroplasts and separated from its fructose-1,6-bisphosphatase counterpart. Experiments with antibodies indicate that the two enzymes are structurally different. 2. Activity of the sedoheptulose-l,7-bisphosphatase enzyme was dependent on M g i+ and a reductant. The most effective reductant tested was thioredoxin that was reduced either photochemi-cally via ferredoxin with chloroplasts or chemically with dithiothreitol. Dithiothreitol added alone also activated the enzyme, but reduced glutathione or 2-mercaptoethanol did not. The thioredoxin-activated enzyme was deactivated by oxidized glutathione. 3. The results suggest that the new substrate-specific sedoheptulose-l,7-bisphosphatase depends on light for activity and resembles certain other regulatory enzymes of the reductive pentose phos­ phate cycle in its mode of regulation. 
  Reference    Z. Naturforsch. 33c, 521 (1978); received M ay 16 1978 
  Published    1978 
  Keywords    Sed-P2ase, Ferredoxin, Thioredoxin, Enzyme Regulation 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0521.pdf 
 Identifier    ZNC-1978-33c-0521 
 Volume    33