-transparent.png){kind=logo}
The processing of human gastric procathepsin E to its mature form, cathepsin E, was studied at pH 3.5. The results revealed the autocatalytic and apparently one-step conversion of procathepsin E to cathepsin E within 10 min of incubation at 14 degrees C under the conditions used. Analyses of the amino acid sequences of both procathepsin E and cathepsin E showed that cleavage occurred at the Met36-Ile37 bond to produce the mature form, cathepsin E. The NH2-terminal amino acid sequence of procathepsin E thus determined was identical with that predicted from the cDNA sequence by Azuma et al. except that the NH2-terminal glutamine residue in the latter was converted into a pyroglutamic acid residue in the former and that the glycine residue at position 2 in the latter sequence was deleted in the former. On the other hand, the NH2-terminal amino acid sequence of cathepsin E was identical with that reported previously by us.
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
January 1995,
Methods in enzymology,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
June 1986,
Biological chemistry Hoppe-Seyler,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
February 2009,
The FEBS journal,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
November 1998,
Biochemical and biophysical research communications,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
October 1999,
FEBS letters,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
February 1998,
The Journal of biological chemistry,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
January 1995,
Advances in experimental medicine and biology,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
February 2005,
FEBS letters,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
May 1993,
FEBS letters,
S B Athauda, and
T Takahashi, and
T Kageyama, and
K Takahashi
October 1989,
The Biochemical journal,
