Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme |
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Authors: | S Yonezawa T Takahashi M Ichinose K Miki J Tanaka S Gasa |
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Institution: | Department of Zoology, Faculty of Science, Hokkaido University, Sapporo, Japan. |
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Abstract: | The amino-terminal structure of rat gastric cathepsin E was identified and compared with the corresponding regions of human procathepsin E and other aspartic proteinases. The alignment revealed that cathepsin E has the most extended amino-terminal structure in aspartic proteinases, thus suggesting that the activation peptide (propeptide) of the human enzyme is 39-residues long. Analysis of oligosaccharide units suggested that rat cathepsin E possesses one N-linked carbohydrate unit, probably of the high mannose type. No evidence was obtained for the presence of O-linked sugars in rat cathepsin E. |
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