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

Biochemical and Biophysical Research Communications
S YonezawaS Gasa

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.

References

Nov 15, 1988·Archives of Biochemistry and Biophysics·S YonezawaN Muto
Aug 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·P L FaustJ M Chirgwin
Dec 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·T ImaiK Murakami

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Citations

Aug 7, 1996·International Journal of Cancer. Journal International Du Cancer·T AzumaM Nakajima
Jan 23, 1991·Biochimica Et Biophysica Acta·S Yonezawa, K Nakamura
Feb 28, 1991·Biochemical and Biophysical Research Communications·S B AthaudaK Takahashi
Nov 8, 2005·Journal of Biochemistry·Yoshiyuki YasudaKenji Yamamoto
Apr 1, 1993·The Journal of Investigative Dermatology·K HaraW L Epstein
Apr 30, 1990·Biochemical and Biophysical Research Communications·S B AthaudaK Takahashi
Jan 8, 2008·Biochemical and Biophysical Research Communications·Nousheen Zaidi, Hubert Kalbacher

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