Dynorphin-degrading cysteine protease is highly specific for paired arginine residues |
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Authors: | T Watanabe S Ishii H Yokosawa |
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Institution: | (1) Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, 060 Sapporo, (Japan) |
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Abstract: | The cleavage of dynorphin and three analogs containing paired basic residues by several proteases was investigated. The cysteine protease of neuroblastoma cells cleaved only the bond between Arg-Arg residues. Submandibular arginylendopeptidase, however, cleaved bonds between both Arg-Arg and Arg-Lys residues, and pancreatic trypsin at the carboxyl sides of both arginine and lysine residues. This shows that the cysteine protease is highly specific for paired arginine residues. |
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Keywords: | Neuropeptide dynorphin paired basic residue neuropeptidase arginylendopeptidase |
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