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1987 (1)
1Author    Horst Beier, LotharF. Fecker, Jochen BerlinRequires cookie*
 Title    Lysine Decarboxylase from H afnia alvei: Purification, Molecular Data and Preparation of Polyclonal Antibodies  
 Abstract    The purification and molecular properties of lysine decarboxylase from Hafnia alvei and the preparation of polyvalent antibodies specific for this enzyme are described. The enzyme was purified within two HPLC steps on a TSK G 4000 SW and a MonoQ column to homogeneity. The subunit of the enzyme has a molecular weight of approximately 80.000 d. Under "native" condi­ tions it seems to form aggregates up to ten subunits. Lysine decarboxylase from H. alvei contains one mol pyridoxal phosphate per mol subunit. Antibodies against the lysine decarboxylase were purified by affinity chromatography. 
  Reference    Z. Naturforsch. 42c, 1307—1312 (1987); received June 5. 1987 
  Published    1987 
  Keywords    Hafnia alvei, Enterobacterium, Lysine Decarboxylase Purification, Characterization 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1307.pdf 
 Identifier    ZNC-1987-42c-1307 
 Volume    42