Display Settings:

Format

Send to:

Choose Destination

    Human cyclophilin has a significantly higher affinity for HIV-1 recombinant p55 than p24.

    Source

    Murex Biotech Ltd., Dartford, Kent, UK. Richard.Bristow@abbott.com

    Abstract

    The ability of cyclophilin to bind a panel of recombinant HIV-gag proteins was assessed using sensitive, quantitative, sandwich enzyme-linked immunosorbant assays (ELISAs). Significantly higher binding to cyclophilin was observed when recombinants contained at least 12 carboxy-terminal amino acids of p17 in addition to p24 sequences. These results indicate that the carboxy-terminus of p17 is important for optimal binding of cyclophilin to p24 and support the theory that cyclophilin acts on the uncleaved HIV-1 gag (p17-p24) precursor.

    PMID:
    10096576
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk