In vitro biosynthesis of the lysosomal cathepsin H

Yukio Nishimura, Keitaro Kato

Research output: Contribution to journalArticle

22 Citations (Scopus)

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 languageEnglish
Pages (from-to)159-164
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume146
Issue number1
DOIs
Publication statusPublished - Jul 15 1987

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Cathepsin H
Biosynthesis
Enzyme Precursors
Membranes
Polyribosomes
Glycoside Hydrolases
Sulfhydryl Compounds
Peptide Hydrolases
In Vitro Techniques
Proteins

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 journalArticle

Nishimura, Yukio ; Kato, Keitaro. / In vitro biosynthesis of the lysosomal cathepsin H. In: Biochemical and Biophysical Research Communications. 1987 ; Vol. 146, No. 1. pp. 159-164.
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