Mitochondrial contribution to protein synthesis in cerebral cortex

H. R. Mahler, Larry Jones, W. J. Moore

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Emetine (at 100 μg/ml) blocks the incorporation of 3H-leucine into the total protein of slices from rat cerebral cortex by > 95%; the block on the synthesis of cytosol proteins is quantitative. Under these conditions protein synthesis resistant to emetine is localized in a mitochondrial fraction that is sensitive to chloramphenicol at 100 μg/ml to the extent of ∼ 70%. We infer that some 15% of the proteins of cerebral cortex mitochondria formed during a 60 min period have been provided by their own protein synthesizing system.

Original languageEnglish
Pages (from-to)384-389
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume42
Issue number3
DOIs
StatePublished - Feb 5 1971

Fingerprint

Cerebral Cortex
Emetine
Proteins
Mitochondria
Chloramphenicol
Leucine
Cytosol
Rats

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Mitochondrial contribution to protein synthesis in cerebral cortex. / Mahler, H. R.; Jones, Larry; Moore, W. J.

In: Biochemical and Biophysical Research Communications, Vol. 42, No. 3, 05.02.1971, p. 384-389.

Research output: Contribution to journalArticle

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