Characterization ofHelicobacter pyloriÏ54promoter-binding activity
نویسندگان
چکیده
منابع مشابه
Synthesis, Characterization, DNA Binding and Nuclease Activity of Cobalt(II) Complexes of Isonicotinoyl Hydrazones
Cobalt(II) complexes of isonicotinoyl hydrazones of two series of ligands have been synthesized and characterized on the basis of elemental analyses, molar conductance, magnetic moment, mass, IR, UV spectral data. Electrochemical behavior of ligands and complexes has been investigated by using cyclic voltammetry. Cyclic voltammetric studies reveal that the oxidation/reduct...
متن کاملEfficient production of nanobodies against urease activity ofHelicobacter pylori in Pichia pastoris.
BACKGROUND/AIM Helicobacter pylori is a major health problem. One of the therapeutic approaches is administration of antibody against H. pylori. The methylotrophic Pichia pastoris is a suitable host for expression of recombinant antibody fragments. The aims of this study were the expression and the evaluation of camelid nanobody in the yeast Pichia pastoris. MATERIALS AND METHODS The camelid-...
متن کاملCharacterization of Transgenic Silkworm Yielded Biomaterials with Calcium-Binding Activity
Silk fibers have many inherent properties that are suitable for their use in biomaterials. In this study, the silk fibroin was genetically modified by including a Ca-binding sequence, [(AGSGAG)6ASEYDYDDDSDDDDEWD]2 from shell nacreous matrix protein. It can be produced as fibers by transgenic silkworm. The Ca-binding activity and mineralization of the transgenic silk fibroin were examined in vit...
متن کاملPotential role ofthiol:disul¢deoxidoreductases in thepathogenesis ofHelicobacter pylori
Helicobacter pylori infections are responsible for a sequence of molecular events which ultimately result in the development of gastric diseases. The pathogenesis of H. pylori has been studied extensively with strong focus on the identification of virulence factors. In contrast, the involvement of thiol:disulfide oxidoreductases in bacterial pathogenesis is less well understood. This paper prov...
متن کاملCharacterization of the nucleotide-binding capacity and the ATPase activity of the PIP3-binding protein JFC1.
In this work, we demonstrate that the phosphatidylinositol 3,4,5-trisphosphate-binding protein JFC1 is an ATP-binding protein with magnesium-dependent ATPase activity. We show that JFC1 specifically binds to the ATP analog 8-azido-[alpha-(32)P]ATP. The affinity of JFC1 for [alpha-(32)P]ATP was 10x greater than its affinity for [alpha-(32)P]ADP; the protein did not appear to bind to [alpha-(32)P...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 2006
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.2006.00258.x