These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characterization of human IgG Fc receptors.
    Author: Vaughn M, Taylor M, Mohanakumar T.
    Journal: J Immunol; 1985 Dec; 135(6):4059-65. PubMed ID: 2933458.
    Abstract:
    A murine monoclonal antibody, KuFc79, has been developed that reacts with human IgG Fc receptors on monocytes, B lymphocytes, and granulocytes. The specificity of KuFc79 for Fc receptors was demonstrated by the ability of Fab fragments to block Fc-mediated phagocytosis by monocytes. This finding was further substantiated by the decrease of KuFc79 binding to monocytes and granulocytes (58 and 70%, respectively) after modulation of surface IgG receptors with aggregated IgG. In addition, Fab KuFc79-conjugated Sepharose was used to isolate functional IgG Fc-binding molecules from soluble extracts of the human monocyte-like cell line U937. By immunoprecipitation, it was further shown that KuFc79 immunoprecipitated molecules of 42,000 and 70,000 daltons from U937 and a human lymphoblastoid cell line, SB. A lower m.w. species of approximately 33,000 was also precipitable from granulocytes. Extensive microheterogeneity of these molecules was noted by isoelectric focusing, which appears to be due to differential sialation.
    [Abstract] [Full Text] [Related] [New Search]