N-terminal amino acid sequences of the heavy and light chains of chicken liver cathepsin L.
Avian cathepsin L (EC 3.4.22.15) was first purified from chicken liver. The enzyme was composed of two polypeptides with Mr values of 28,000 (heavy chain) and 5000 (light chain). The two polypeptide chains of the enzyme were separated by gel filtration after cleavage of disulfide bonds. The N-terminal amino acid sequences of the heavy and light chains were (sequence in text) and (sequence in text) respectively. These sequences show high homologies with those of the N-terminal and C-terminal portions of papain, respectively. The residues of the surrounding area of cysteine-25 in the heavy chain were quite similar to those in the region around the active-site cysteine of papain.
D000595:Amino Acid Sequence; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000302:isolation & purification*; D002645:Chickens; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010206:Papain
D046911:Macromolecular Substances; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; D010206:Papain