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Amino acid sequences of the human kidney cathepsins H and L
Author(s) -
Ritonja Anka,
Popović Tatjana,
Kotnik Matjaž,
Machleidt Werner,
Turk Vito
Publication year - 1988
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(88)80028-0
Subject(s) - cyanogen bromide , cathepsin o , cathepsin h , cathepsin a , cathepsin , biochemistry , peptide sequence , cathepsin e , amino acid , chemistry , cleavage (geology) , cathepsin l , papain , microbiology and biotechnology , cathepsin b , cathepsin c , biology , enzyme , gene , paleontology , fracture (geology)
The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined. Cathepsin H contains 230 residues and has an M r of 25 116. The sequence was obtained by sequencing the light, heavy and mini chain and the peptides produced by cyanogen bromide cleavage of the single‐chain form of the enzyme. The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an M r of 23720. Its amino acid sequence was deduced from N‐terminal sequences of the heavy and light chains and from the sequences of cyanogen bromide fragments of the heavy chain. The fragments were aligned by comparison with known sequences of cathepsins H and L from other species. Cathepsins H and L exhibit a high degree of sequence homology to cathepsin B (EC 3.4.22.1) and other cysteine proteinases of the papain superfamily.