title: Molecular and functional properties of EF-Tu from Calderobacterium hydrogenophilum.
abstract: Protein synthesis elongation factor Tu (EF-Tu) was purified from an extreme thermophilic hydrogen-oxidizing bacterium Calderobacterium hydrogenophilum. The relative molecular mass of EF-Tu. GDP was 51,000. The factor was heat stable and lost only 50% of its activity after heating at 80 degrees C for 5 min. Native and reduced EF-Tu or EF-Tu. GDP contained one SH-reactive group. The elongation factors from C. hydrogenophilum and E. coli were shown to be immunologically identical. From the Southern hybridization analysis seems to suggest that chromosome DNA of C. hydrogenophilum has two tuf genes.
authors.affiliation: Institute of Zoology, Academia Sinica, Beijing, China.
authors.forename: C L
authors.initials: CL
authors.lastname: Qiao
mesh_terms: D004269:DNA, Bacterial / Q000032:analysis; D004926:Escherichia coli / Q000737:chemistry; D005798:Genes, Bacterial; D005779:Immunodiffusion; D008970:Molecular Weight; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D015183:Restriction Mapping; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics
chemical_list: D004269:DNA, Bacterial; D010444:Peptide Elongation Factor Tu