rubella/グルタチオン

Extensive subfunctionalization might explain why so many genes have been maintained after gene duplication, which provides the engine for gene family expansion. However, it is still a particular challenge to trace the evolutionary dynamics and features of functional divergences in a supergene family

BACKGROUND Until rubella is eradicated there will be a continuing need for rubella antibody surveillance. Antigen production using recombinant DNA technology may be a viable alternative to traditional techniques of producing antigens for enzyme immunoassays (EIAs). OBJECTIVE To investigate the

The replicative proteins of Rubella virus are generated from a polyprotein that is translated from the 5'-terminal segment of the viral genome. The determination of the genome sequence and the description of amino acid sequence motifs which are proposed to be characteristic for helicase proteins

The determination of neomycin sulfate was made using photoluminescent amino-functionalized graphene quantum dots (obtained from hydro-exfoliation of a mixture of citric acid and glutathione). From the several ions tested, Fe³⁺ was the best mediator to enable an off/on photoluminescence

Serological assays detecting antibodies in serum or plasma samples are useful and versatile instruments to investigate an individual's infection and vaccination history, e.g. for clinical diagnosis, personal risk evaluation, and seroepidemiological studies. Multiplex Serology is a suspension bead

Two glutathione S-transferase fusion proteins containing 44 (p1503) and 75 (p1509) amino acid residues of the rubella virus E1 glycoprotein were expressed in Escherichia coli with the aim of producing a recombinant rubella virus antigen for use in serological assays. p1503 contained three

To prepare an epitope-based recombinant Rubella virus (RV) recombinant diagnostic antigen(designated ‘H29’) and preliminarily evaluate its antigenicity. With Glutathione S-Transferase (GST) located at the N-terminal, and the His tag at the C-terminal, the epitope-based RV recombinant diagnostic

A proline-rich region (PRR) within the rubella virus (RUBV) P150 replicase protein that contains three SH3 domain-binding motifs (PxxPxR) was investigated for its ability to bind cell proteins. Pull-down experiments using a glutathione S-transferase-PRR fusion revealed PxxPxR motif-specific binding

OBJECTIVE Bioprocess oxidative stress caused by many reactive oxygen species (ROS) can lead to largely irreversible perturbation of yeast bioprocesses. These include the production of proteins derived from recombinant DNA yeast technology (aerobically grown Saccharomyces cerevisiae). These proteins