Lysine Decarboxylase from Hafnia alvei: Purification, Molecular Data and Preparation of Polyclonal Antibodies
نویسندگان
چکیده
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.
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