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Experimental study demonstrates cross-reactivity of mouse ornithine decarboxylase antibodies in rodent tissues, indicating structural conservation across mammalian enzymes.
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.
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Persson et al. (1982) studied this question.
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