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J. Biochem, 1988, Vol. 104, No. 3 472-476
© 1988 Japanese Biochemical Society

research-article

Purification and Characterization of Chicken Liver Cathepsin B1

Kenji Wada and Tadashi Tanabe2

Laboratory of Cell Biology, National Cardiovascular Center Research Institute Suita, Osaka 565

2To whom correspondence should be addressed

Cathepsin B was purified, 400-fold, to homogeneity from chicken liver. The enzyme comprised a mixture of two kinetically indistinguishable forms (approximately 1: 1), which were separated on concanavalin A (Con A)-Sepharose; one consisting of Mr 25,500 and 5,000 polypeptide chains bound to Con A-Sepharose but the other, composed of Mr 24,500 and 5,000 polypeptide chains, did not. N-terminal amino acid sequence analyses of a mixture of the Mr 25,500 and 24,500 polypeptide chains, and of the Mr 5,000 polypeptide chain revealed single amino acid sequences, respectively. These amino acid sequences were homologous to those of the heavy and light chains of mammalian enzymes, respectively. The chicken liver and mammalian cathepsin B were similar in structure and properties.

1This work was supported in part by grants from the Ministry of Education, Science and Culture, and the Ministry of Health and Welfare of Japan. Portions of this paper (including "MATERIALS AND METHODS," Table IS, and Figs. 1S to 3S) are presented as a miniprint at the end of this paper.


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