Báo cáo khoa học: 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
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To study the roles of the catalytic activity, propeptide, and N-glycosylationof the intracellular aspartic proteinase cathepsin E in biosynthesis, process-ing, and intracellular trafficking, we constructed various rat cathepsin Emutants in which active-site Asp residues were changed to Ala or whichlacked propeptides and N-glycosylation.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: 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
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: 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
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