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Primary structure of bovine cathepsin S Comparison to cathepsins L, H, B and papain
Author(s) -
Wiederanders Bernd,
Broemme Dieter,
Kirschke Heidrun,
Kalkkinen Nisse,
Rinne Ari,
Paquette Thomas,
Toothman Penelope
Publication year - 1991
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(91)80971-5
Subject(s) - cathepsin o , cathepsin h , cathepsin l1 , cathepsin , cathepsin a , peptide sequence , cathepsin e , biochemistry , protein primary structure , amino acid , microbiology and biotechnology , cathepsin b , cathepsin l , cathepsin c , biology , papain , complementary dna , open reading frame , chemistry , enzyme , gene
The primary structure of bovine cathepsin S was determined by combining results of protein and peptide sequencing with the sequence deduced from nucleic acid sequencing. Using polymerase chain reaction (PCR) technology, cDNA clones commencing at amino acid 22 of the mature enzyme and continuing through the 3′ untranslated region of bovine cathepsin S mRNA were isolated and sequenced. The open reading frame in these overlapping clones correctly predicts the determined amino acid sequence of 13 tryptic peptides derived from purified bovine spleen cathepsin S. The deduced amino acid sequence shows that mature bovine cathepsin S consists of 217 amino acids corresponding to a molecular weight of 23.7 kDa. Cathepsin S belongs to the papain superfamily of lysosomal cysteine proteinases and shares 41% identity with papain. Amino acid sequence identities of bovine cathepsin S to human cathepsins L, H, and B are 56%, 47% and 31% respectively.