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J. Biochem, 1984, Vol. 96, No. 5 1525-1530
© 1984 Japanese Biochemical Society

research-article

A Monoclonal Antibody to Rat Liver Ornithine Decarboxylase1

Senya MATSUFUJI, Kazunobu FUJITA2, Takaaki KAMEJI, Ryuhei KANAMOTO, Yasuko MURAKAMI and Shin-ichi HAYASHI

Department of Nutrition, The Jikei University School of Medicine Minato-ku, Tokyo 105

A monoclonal antibody was obtained against rat liver ornithine decarboxylase by using hybridoma technology with a small amount of partially purified enzyme. The antibody, IgG1 of k-type, was affinity-purified to homogeneity from culture supernatants of hybridoma cells. While the antibody had no inhibitory effect on ornithine decarboxylase activity when tested alone, it precipitated up to 87 units (60 ng) of the enzyme per microgram in the presence of formalin-fixed Staphylo-coccus aureus Cowan I bacteria. Immunoadsorption on a column of the monoclonal antibody-Sepharose 4B was shown to be useful for the removal of ornithine decarboxylase from antizyme inhibitor preparations, an essential procedure for the accurate assay of either ornithine decarboxylase-antizyme complex or antizyme inhibitor. It was also shown that antizyme could be affinity-purified by using a column of the monoclonal antibody-Affi-Gel 10 to which ornithine decarboxylase had been bound.

1 This study was supported in part by Grants-in-Aid for Scientific Research (57480158, 58770230) from the Ministry of Education, Science and Culture of Japan.

2Present address: Department of Microbiology, Jikei University School of Medicine, Minato-ku, tokyo 105


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