Cystic fibrosis factor activity (CFFA), assayed as the ability to stop oyster ciliary movement, was present in serum-free medium from actively growing cystic fibrosis skin fibroblast cultures. CFFA was associated with a low molecular weight, negatively charged molecule that contained no uronic acid and was heat and pH labile. When CFFA-positive media were mixed with human IgG1, the CFFA was chromatographically displaced and emerged with the IgG1 fraction on column chromatography. Experiments in which various immunoglobulins were added to CFFA-positive culture media and then incubated with specific anti-immunoglobulins suggested that CFFA binding was class specific for human IgG, subclass specific for IgG1 and IgG2, and occurred with intact unaggregated heavy chains but not with κ- and λ-light chains, or Fab, Fc, and F(ab')2 fragments. The serum protein ß2-microglobulin, which has structural homology to IgG, also bound CFFA.
CHARACTERIZATION OF CYSTIC FIBROSIS FACTOR AND ITS INTERACTION WITH HUMAN IMMUNOGLOBULIN
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B. Shannon Danes, Stephen D. Litwin, Thomas H. Hütteroth, Hartwig Cleve, Alexander G. Bearn; CHARACTERIZATION OF CYSTIC FIBROSIS FACTOR AND ITS INTERACTION WITH HUMAN IMMUNOGLOBULIN . J Exp Med 1 June 1973; 137 (6): 1538–1543. doi: https://doi.org/10.1084/jem.137.6.1538
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