Abstract
Globin synthesis in cell-free extracts of rabbit reticulocytes was carried out in the presence of 3H-labeled hemin. Sucrose gradient centrifugation analysis revealed [3H]hemin in the polyribosome fraction. The addition of puromycin resulted in the release of both [3H]hemin- and [14C]leucine-labeled polypeptide from the polyribosomes. The data suggest cotranslational folding of the globin molecule on the ribosome and cotranslational heme binding to the nascent globin chain. © 1993.
| Original language | English |
|---|---|
| Pages (from-to) | 261-263 |
| Number of pages | 3 |
| Journal | FEBS Letters |
| Volume | 326 |
| Issue number | 1-3 |
| DOIs | |
| State | Published - Jan 1 1993 |
Keywords
- Attachment
- Cotranslational folding
- Heme
- Hemoglobin
- Nascent peptide
Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver