Journal article
Mitochondrial protein synthesis: Resistance to emetine and response to RNA synthesis inhibitors
Biochemical and Biophysical Research Communications, Vol.40(4), pp.941-948
1970
DOI: 10.1016/0006-291X(70)90994-0
PMID: 5495740
Abstract
Mitochondrial protein synthesis is not inhibited by concentrations of emetine that completely suppress cytoplasmic protein synthesis. The emetine resistant, chloramphenicol sensitive structures sediment in a broad band about 95S and in a sharp band at 55S after brief treatment with RNAse. The activity of the structures has a half-life of 3 hours in cordycepin or actinomycin D and of less than 30 minutes in ethidium bromide.
Details
- Title: Subtitle
- Mitochondrial protein synthesis: Resistance to emetine and response to RNA synthesis inhibitors
- Creators
- S PerlmanS Penman
- Resource Type
- Journal article
- Publication Details
- Biochemical and Biophysical Research Communications, Vol.40(4), pp.941-948
- DOI
- 10.1016/0006-291X(70)90994-0
- PMID
- 5495740
- NLM abbreviation
- Biochem Biophys Res Commun
- ISSN
- 0006-291X
- eISSN
- 1090-2104
- Publisher
- Elsevier Inc
- Grant note
- DOI: 10.13039/100000002, name: National Institutes of Health, award: GB-5809; DOI: 10.13039/100000001, name: National Science Foundation
- Language
- English
- Date published
- 1970
- Academic Unit
- Microbiology and Immunology; Stead Family Department of Pediatrics; Iowa Neuroscience Institute; Infectious Disease (Pediatrics)
- Record Identifier
- 9983777355902771
Metrics
31 Record Views