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Interactions between "Fever" Proteins and Normal Serum Proteins in Febrile Cancer Patients¹

The Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, New York 10021

When analyzed by cationic discontinuous electrophoresis in urea-containing polyacrylamide gels, plasma or serum from febrile individuals contains trace quantities of five protein bands that are not recognizable in the blood of normal individuals. These proteins appear and disappear in parallel in sequential samples. Cerebrospinal fluid from febrile and nonfebrile individuals contains a protein band that is electrophoretically identical with only one of these proteins. Since the trace proteins migrate, in urea-containing polyacrylamide gel electrophoresis, as if they had a molecular size of 30,000 daltons, their absence from cerebrospinal fluid implies the existence, in vivo, of interactions between them and other serum proteins. Under nondissociating conditions, four of the bands appear to circulate in physical interaction with one another. In molecular sieve chromatography at neutral pH in lipid-free sera, the trace proteins have an approximate molecular size of 165,000 daltons; in lipemic sera they have a molecular weight of 200,000 daltons. Their behavior in gel filtration and in ionexchange chromatography excludes extensive interaction with any of the following: immunoglobulin M, immunoglobulin G, ₂-macroglobulin, haptoglobin, and albumin. Interactions between these and other serum proteins are reduced by high concentrations of urea and by low pH. The mechanisms responsible for the observed protein-protein associations would appear to include electrostatic attraction, hydrogen bonding, and weak hydrophobic interaction.

¹ This work was supported in part by Grants from the Bodman Foundation and DeDombrowski Fund and by Grants CA 08748 and CA 15928 from the National Cancer Institute.

Received 11/24/76. Accepted 2/ 3/77.