Article
Characterization of rat cathepsin E and mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells.
The FEBS journal - 1 Jan 2006
Tsukuba Takayuki, Ikeda Shinobu, Okamoto Kuniaki, Yasuda Yoshiyuki, Sakai Eiko, Kadowaki Tomoko, Sakai Hideaki, Yamamoto Kenji
Abstract excerpt
To study the roles of the catalytic activity, propeptide, and N-glycosylation of the intracellular aspartic proteinase cathepsin E in biosynthesis, processing, and intracellular trafficking, we constructed various rat cathepsin E mutants in which active-site Asp residues were changed to Ala or which lacked propeptides and N-glycosylation. Wild-type cathepsin E expressed in human embryonic kidney 293T cells was...
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