In vitro biosynthesis of the lysosomal cathepsin H

Yukio Nishimura, Keitaro Kato

研究成果: Contribution to journalArticle査読

22 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)159-164
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
146
1
DOI
出版ステータス出版済み - 7 15 1987

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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