Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053400 | FEBS Letters | 2005 | 7 Pages |
Abstract
Galectin-9 and galectin-8, members of β-galactoside-binding animal lectin family, are promising agents for the treatment of immune-related and neoplastic diseases. The proteins consist of two carbohydrate recognition domains joined by a linker peptide, which is highly susceptible to proteolysis. To increase protease resistance, we prepared mutant proteins by serial truncation of the linker peptide. As a result, mutant forms lacking the entire linker peptide were found to be highly stable against proteolysis and retained their biological activities. These mutant proteins might be useful tools for analyzing the biological functions and evaluating the therapeutic potential of galectin-9 and galectin-8.
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Authors
Nozomu Nishi, Aiko Itoh, Aimi Fujiyama, Naoko Yoshida, Shin-ichi Araya, Mitsuomi Hirashima, Hiroki Shoji, Takanori Nakamura,