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 |
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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 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology