The subunits in rabbit anti-Forssman IgM antibody.

Published

Journal Article

Rabbit IgM anti-Forssman antibody was highly purified and the subunits obtained on reduction and alkylation were labeled radioactively and isolated by two different and unrelated methods. In both cases the subunits were found to have a molecular weight of about 90,000, based on their behavior on density gradient centrifugation and gel filtration, and evidence is given that they contained one light and one heavy chain. The subunits bound only weakly to sheep erythrocyte stroma, and only half could be shown to possess antigen specific sites. The data are consistent with the concept that each anti-Forssman IgM molecule has five effective binding sites, but it is uncertain whether the ineffectiveness of the remaining five H-L chain pairs is inherent in the structure of the IgM molecule or an artifact due to the isolation procedure. Intact IgM anti-Forssman antibody binds very firmly to structures containing multiple repeating antigen sites, and it appears that this is due to the presence of multiple binding sites on the molecule.

Full Text

Duke Authors

Cited Authors

  • Frank, MM; Humphrey, JH

Published Date

  • May 1, 1968

Published In

Volume / Issue

  • 127 / 5

Start / End Page

  • 967 - 982

PubMed ID

  • 5655105

Pubmed Central ID

  • 5655105

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.127.5.967

Language

  • eng

Conference Location

  • United States