| Autor: |
Kishi, Kenji, Yamazaki, Kazuya, Yasuda, Ikuko, Yahagi, Naohisa, Ichinose, Masao, Tsuchiya, Yuichi, Athauda, Senarath B.P., Inoue, Hideshi, Takahashi, Kenji |
| Předmět: |
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| Zdroj: |
Journal of Biochemistry; 2001, Vol. 130 Issue 3, p425-430, 6p |
| Abstrakt: |
Previously we isolated and characterized a membrane-bound, arginine-specific serine protease from pig intestinal mucosa [J. Biol Chem 269, 32985–32991 (1994)]. For further characterization of this type of enzyme, we cloned a cDNA from rat intestinal mucosa encoding the precursor of a similar protease. The partial amino acid sequences determined for the pig enzyme were found to be shared almost completely by the rat enzyme. The serine protease domain of the rat enzyme, heterologously expressed in Escherichia coli, specifically cleaved Arg (or Lys)-X bonds with a marked preference for Arg-Arg or Arg-Lys, similar to the pig enzyme. The mRNA for the rat enzyme was shown to be distributed mainly in intestine, and the enzyme was detected in the duodenal mucosa as a 70 kDa protein. Immunohistochemical analysis of the small intestinal tissue showed that the enzyme is localized mainly on brushborder membranes. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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