In vitro synthesis of thymosin beta 4 encoded by rat spleen mRNA
| Autor: | Aleksandra Wodnar Filipowicz, B. L. Horecker |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
chemistry.chemical_classification
Multidisciplinary Cell-Free System Thymosin Peptide Biology Molecular biology Rats Amino acid Thymus Hormones Thymosin beta-4 medicine.anatomical_structure Reticulocyte chemistry Biochemistry Protein Biosynthesis medicine Protein biosynthesis Animals RNA Messenger Beta (finance) Polyacrylamide gel electrophoresis Spleen Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 80:1811-1815 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.80.7.1811 |
| Popis: | Thymosin beta 4, containing 43 amino acids and acetylated at the NH2 terminus, is synthesized in vitro in a rabbit reticulocyte lysate or in a yeast protein-synthesis system in the presence of mRNA from rat spleen. The product formed was identified as beta 4 by immunoprecipitation by a specific anti-beta 4 antiserum, comigration with authentic beta 4 in NaDodSO4/polyacrylamide gel electrophoresis and in HPLC, and identity of peptide fragments. The immunoprecipitable product generated in the wheat germ protein-synthesizing system emerged slightly ahead of beta 4 in HPLC and appeared to lack the NH2-terminal acetyl group. There was no evidence for formation of a larger polypeptide precursor of beta 4 in any of the three systems used. In sucrose density gradient centrifugation, the mRNA coding for beta 4 was recovered in the 7-8S mRNA fraction. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|