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Molecular cloning and sequencing of cDNA for rat cathepsin H Homology in pro‐peptide regions of cysteine proteinases
Author(s) -
Ishidoh Kazumi,
Imajoh Shinobu,
Emori Yasufumi,
Ohno Shigeo,
Kawasaki Hiroshi,
Minami Yasufumi,
Kominami Eiki,
Katunuma Nobuhiko,
Suzuki Koichi
Publication year - 1987
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(87)80545-8
Subject(s) - complementary dna , cloning (programming) , homology (biology) , microbiology and biotechnology , molecular cloning , cathepsin l , biology , cathepsin , peptide , cysteine , biochemistry , chemistry , gene , enzyme , computer science , programming language
A cDNA for rat cathepsin H was isolated and sequenced. The deduced protein comprising 333 amino acid residues is composed of a typical signal sequence (21 residues), a pro‐peptide region (92 residues) and a mature enzyme region (220 residues). The amino acid sequence in the pro‐peptide region, in particular, residues Phe‐(−41) to Ser‐(−29) of cathepsin H, is highly homologous to the pro‐peptide regions of other cysteine proteinases. This homologous region may play a role in the processing of cysteine proteinases.