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    FEBS Lett. 1987 Oct 19;223(1):69-73.

    Molecular cloning and sequencing of cDNA for rat cathepsin L.

    Ishidoh K, Towatari T, Imajoh S, Kawasaki H, Kominami E, Katunuma N, Suzuki K.

    Department of Enzyme Chemistry, University of Tokushima, Japan.

    A near full-length cDNA for rat cathepsin L was isolated. The deduced protein comprises 334 amino acid residues (Mr 37,685) containing a typical signal sequence (N-terminal 17 residues), pro-peptide (96 residues), and the sequence for mature cathepsin L (221 residues). Rat cathepsin L shows 94% amino acid identity with mouse cysteine proteinase. Amino acid sequence homologies of rat cathepsin L with rat cathepsins H and B are 45 and 25%, respectively. These facts indicate that mouse cysteine proteinase is probably mouse cathepsin L and that cathepsin L is more closely related to cathepsin H than cathepsin B.

    PMID: 3666143 [PubMed - indexed for MEDLINE]

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