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'Prolyl Endopeptidase Soluble extracts' in keywords
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1994 (1)
1Author    Ulrike Strohmeier, ChristianG. Erdes3, Wolfgang LockaubRequires cookie*
 Title    Proteolysis in Heterocyst-Forming Cyanobacteria: Characterization of a Further Enzyme with Trypsin-Like Specificity, and of a Prolyl Endopeptidase from Anabaena variabilis  
 Abstract    of the cyanobacterium Anabaena variabilis ATCC 29413 and an en­ gineered mutant that lacks an intracellular protease cleaving after Lys and Arg (Maldener, Lockau, Cai, and Wolk, Mol. Gen. Genet. 225, 113-120 (1991)) were separated by ion ex­ change chromatography, and protease profiles determined using azocasein, Na-benzoyl-D,L-arginine-4-nitroanilide and N-carbobenzoxy-glycyl-L-proline-4-nitroanilide as substrates. A second enzyme cleaving at the carboxyl side of lysine and arginine, and a prolyl endopepti­ dase were detected, enriched and characterized. Both proteolytic enzymes appear to be located in the periplasm. 
  Reference    Z. Naturforsch. 49c, 70—78 (1994); received September 29/December 81993 
  Published    1994 
  Keywords    Anabaena variabilis, Cyanobacterium, Heterocysts, Proteolytic Enzymes, Prolyl Endopeptidase Soluble extracts 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0070.pdf 
 Identifier    ZNC-1994-49c-0070 
 Volume    49