Selected article for: "high concentration and low concentration"
Author: Changhai Lei; Wenyan Fu; Kewen Qian; Tian Li; Sheng Zhang; Min Ding; Shi Hu
Title: Potent neutralization of 2019 novel coronavirus by recombinant ACE2-Ig
  • Document date: 2020_2_2
    • ID: aeuy92bx_5
    Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.02.01.929976 doi: bioRxiv preprint ~ 4 ~ assays (Fig. S1 ) and both fusion proteins showed high affinity to RBDs. Moreover, the fusion proteins had similar denaturation temperature compared with the Fc fusion protein TIGIT-Ig reported in our pervious report 13 , suggesting a IgG-like stability. The lowest concentration (< 2%) of high molecul.....
    Document: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.02.01.929976 doi: bioRxiv preprint ~ 4 ~ assays (Fig. S1 ) and both fusion proteins showed high affinity to RBDs. Moreover, the fusion proteins had similar denaturation temperature compared with the Fc fusion protein TIGIT-Ig reported in our pervious report 13 , suggesting a IgG-like stability. The lowest concentration (< 2%) of high molecular weight and low molecular weight products was observed after 1 week of storage at 40 °C at a 1 mg/ml concentration. Pharmacokinetic (PK) parameters of the fusion proteins were then tested in our study. Mice were treated separately with a single intravenous dose of fusion proteins and the serum concentrations of fusion proteins were determined by ELISA. The results showed that the main PK parameters of ACE2-Ig, mACE2-Ig and TIGIT-Ig were very similar in mice and demonstrated the high stability of the fusion proteins. The experimental data are summarized in Table S1 .

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