| Literature DB >> 7164704 |
Abstract
L-Ornithine decarboxylase was purified to apparent homogeneity from the kidneys of testosterone-treated mice. Antibodies to ornithine decarboxylase were raised in a rabbit using the purified enzyme. Ouchterlony double diffusion technique revealed a single precipitin line between the antiserum and purified mouse kidney ornithine decarboxylase. The antibodies inhibited ornithine decarboxylase from various tissues of mice and rats to the same extent, indicating a close immunological relationship. S-Adenosyl-L-methionine decarboxylase and L-histidine decarboxylase from mouse kidney as well as ornithine decarboxylase from Escherichia coli were unaffected by the antibodies.Entities:
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Year: 1982 PMID: 7164704 DOI: 10.3891/acta.chem.scand.36b-0685
Source DB: PubMed Journal: Acta Chem Scand B ISSN: 0302-4369