The Journal of Experimental Medicine, Vol 137, 1538-1543,
Copyright © 1973 by The Rockefeller University Press
CHARACTERIZATION OF CYSTIC FIBROSIS FACTOR AND ITS INTERACTION WITH HUMAN IMMUNOGLOBULIN
B. Shannon Danes 1,
Stephen D. Litwin 1,
Thomas H. Hütteroth 1,
Hartwig Cleve 1, and
Alexander G. Bearn 1
1 From the Division of Human Genetics, Department of Medicine, Cornell University Medical College, New York 10021
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 
- and 
-light chains, or Fab, Fc, and F(ab')2 fragments. The serum protein ß2-microglobulin, which has structural homology to IgG, also bound CFFA.
Submitted on April 1, 1973
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