Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa

Kenji Kishi, Kazuya Yamazaki, Ikuko Yasuda, Naohisa Yahagi, Masao Ichinose, Yuichi Tsuchiya, Senarath B.P. Athauda, Hideshi Inoue, Kenji Takahashi

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)425-430
Number of pages6
JournalJournal of biochemistry
Issue number3
Publication statusPublished - 2001
Externally publishedYes


  • Brushborder membrane
  • Intestinal mucosa
  • Serine protease
  • Subcellular localization
  • Substrate specificity

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa'. Together they form a unique fingerprint.

Cite this