In vitro biosynthesis of the lysosomal cathepsin H

Yukio Nishimura, Keitaro Kato

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)


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 languageEnglish
Pages (from-to)159-164
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Jul 15 1987

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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