Molecular cloning and sequencing of cDNA for rat cathepsin L

FEBS Letters

Towatari, Takae²  Katunuma, Nobuhiko²  Kawasaki, Hiroshi¹  Imajoh, Shinobu¹  Kominami, Eiki²  Suzuki, Koichi¹  Ishidoh, Kazumi² 

[1] Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, 3-18 Honkomagome, Bunkyo-ku, Tokyo 113, Japan;Department of Enzyme Chemistry, Institute of Enzyme Research, The University of Tokushima, Tokushima 770, Japan

关键词: Cathepsin L;    Cysteine proteinase;    cDNA cloning;    Amino acid sequence;    Proenzyme;    Lysosome;    bp;    base pairs;    HPLC;    high-performance liquid chromatography;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    Con A;    concanavalin A;    MCP;    mouse cysteine proteinase;   

DOI  :  10.1016/0014-5793(87)80511-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A near full-length cDNA for rat cathepsin L was isolated. The deduced protein comprises 334 amino acid residues (M _r 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.

【 授权许可】

Unknown