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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme.

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.[1]

References

  1. Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme. Yonezawa, S., Takahashi, T., Ichinose, M., Miki, K., Tanaka, J., Gasa, S. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
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