Characterization of cystic fibrosis factor and its interaction with human immunoglobulin

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...

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Bibliographic Details
Published in:The Journal of experimental medicine 1973-06, Vol.137 (6), p.1538-1543
Main Authors: Danes, B S, Litwin, S D, Hütteroth, T H, Cleve, H, Bearn, A G
Format: Article
Language:English
Subjects:
Age Factors
Antigen-Antibody Reactions
Brief Definitive Reports
Cell Line
Cells, Cultured
Cystic Fibrosis - immunology
Fibroblasts - analysis
Fibroblasts - immunology
Humans
Immunoglobulin G - analysis
Immunoglobulins - analysis
Skin - immunology
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Summary: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 kappa- and lambda-light chains, or Fab, Fc, and F(ab')(2) fragments. The serum protein beta(2)-microglobulin, which has structural homology to IgG, also bound CFFA.
ISSN:0022-1007
1540-9538
DOI:10.1084/jem.137.6.1538