Intracellular site of synthesis of microsomal heme oxygenase in pig spleen

Shigeki Shibahara, Tadashi Yoshida, Goro Kikuchi

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

In the pig spleen the specific activity of heme oxygenase was two to three times higher in smooth microsomes than in rough microsomes, whereas the total heme oxygenase activities recovered in the two microsomal fractions were similar. Free and bound polysomes were isolated from pig spleen and nascent peptides on these polysomes were analyzed by employing [3H]puromycin and a heme oxygenase-specific rabbit antibody (IgG). It was shown that free polysomes are the major site of heme oxygenase synthesis. In addition, cell-free synthesis of heme oxygenase was performed in a reticulocyte lysate system with free and bound polysomes isolated from pig spleen, and the results obtained again indicated that heme oxygenase is synthesized predominantly on free polysomes. The heme oxygenase newly synthesized on free polysomes may be incorporated first into the rough portion of endoplasmic reticulum either before or after its release from polysomes, although the specific activity of this enzyme at the steady state is considerably higher in the smooth region.

Original languageEnglish
Pages (from-to)45-50
Number of pages6
JournalJournal of biochemistry
Volume88
Issue number1
Publication statusPublished - 1980 Jul 1

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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