Abstract
A lysosomal thiol protease cathepsin H has been synthesized in vitro and shown to undergo co-translational segregation into the lumen of microsomal vesicles. Using cell-free synthesis, a 36 K Da cathepsin H was found to be synthesized exclusively on membrane-bound polysomes. When the microsomal membranes were present during translation, a glycosylated 41 K Da proenzyme appeared in the microsomal lumen. This proenzyme was converted to a 34 K Da protein by endoglycosidase H treatment. These results suggest that the nascent chain of cathepsin H has a transient N-terminal prepropeptide.
| Original language | English |
|---|---|
| Pages (from-to) | 159-164 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 146 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jul 15 1987 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
In vitro biosynthesis of the lysosomal cathepsin H. / Nishimura, Yukio; Kato, Keitaro.
In: Biochemical and Biophysical Research Communications, Vol. 146, No. 1, 15.07.1987, p. 159-164.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - In vitro biosynthesis of the lysosomal cathepsin H
AU - Nishimura, Yukio
AU - Kato, Keitaro
PY - 1987/7/15
Y1 - 1987/7/15
N2 - A lysosomal thiol protease cathepsin H has been synthesized in vitro and shown to undergo co-translational segregation into the lumen of microsomal vesicles. Using cell-free synthesis, a 36 K Da cathepsin H was found to be synthesized exclusively on membrane-bound polysomes. When the microsomal membranes were present during translation, a glycosylated 41 K Da proenzyme appeared in the microsomal lumen. This proenzyme was converted to a 34 K Da protein by endoglycosidase H treatment. These results suggest that the nascent chain of cathepsin H has a transient N-terminal prepropeptide.
AB - A lysosomal thiol protease cathepsin H has been synthesized in vitro and shown to undergo co-translational segregation into the lumen of microsomal vesicles. Using cell-free synthesis, a 36 K Da cathepsin H was found to be synthesized exclusively on membrane-bound polysomes. When the microsomal membranes were present during translation, a glycosylated 41 K Da proenzyme appeared in the microsomal lumen. This proenzyme was converted to a 34 K Da protein by endoglycosidase H treatment. These results suggest that the nascent chain of cathepsin H has a transient N-terminal prepropeptide.
UR - http://www.scopus.com/inward/record.url?scp=0023655466&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023655466&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(87)90705-4
DO - 10.1016/0006-291X(87)90705-4
M3 - Article
C2 - 3606613
AN - SCOPUS:0023655466
VL - 146
SP - 159
EP - 164
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -