Purification and characterization of chicken liver cathepsin B.
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.
Wada
K
K
Laboratory of Cell Biology, National Cardiovascular Center Research Institute, Osaka.
Tanabe
T
T
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002401:Cathepsin B / Q000032:analysis / Q000302:isolation & purification*; D002645:Chickens; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data
D000596:Amino Acids; D002401:Cathepsin B; D000103:Acetyl-CoA Carboxylase