These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: A fast and effective method for purification of elongation factor 1 alpha from rabbit liver. Author: Shalak VF, Budkevich TV, Negrutskił BS, El'skaia AV. Journal: Ukr Biokhim Zh (1978); 1997; 69(2):104-9. PubMed ID: 9463227. Abstract: Fast, efficient and gentle method of elongation factor 1 alpha (EF-1 alpha) purification from rabbit liver has been developed. Isolation procedure consists of three steps: gel-filtration of postmithohondrial supernatant on Sephacryl S-400, anion(DEAE-Cellulose)- and cation(SP-Sepharose)- exchange chromatographies. The procedure takes two-three days. Minimal number of the purification steps and the only one buffer usage during entire purification provide the high speed and efficiency of the method. Purity of EF-1 alpha preparation obtained was more than 90% as judged from DS-Na polyacrylamide gel electrophoresis. EF-1 alpha was demonstrated to be highly active in three different assays: the [3H]GDP-binding, the stimulation of [14C]phenylalanyl-tRNA binding to poly(U)-programmed 80S ribosomes and the stimulation of poly[14C]phenylalanine synthesis on poly(U)-programmed 80S ribosomes in the presence of EF-2. Since EF-1 alpha may exist in a cell as either GDP- or GTP-bound form the nature of nucleotide bound was studied using high pressure liquid chromatography (HPLC) analysis. Each molecule of EF-1 alpha appears to contain one molecule of GDP.[Abstract] [Full Text] [Related] [New Search]