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N‐terminal amino acid sequences of the heavy and light chains of chicken liver cathepsin L
Author(s) -
Wada Kenji,
Tanabe Tadashi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81137-1
Subject(s) - papain , cysteine , cleavage (geology) , immunoglobulin light chain , cathepsin , chicken liver , chemistry , amino acid , amino acid residue , cathepsin l , size exclusion chromatography , polypeptide chain , biochemistry , enzyme , peptide sequence , stereochemistry , biology , paleontology , fracture (geology) , gene , antibody , immunology
Avian cathepsin L (EC 3.4.22.15) was first purified from chicken liver. The enzyme was composed of two polypeptides with M r 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 APRSVDWREKGYVTPVKDQGQCGSCWAFSTTGALEGQ and GKKYWIVKNSWGEKWGDKGYIYMAKDRKNHCGIATAASYP, 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.