Cryoglobulinemia

Autor: Demetrios A. Rigas, Roy Laver Swank, Arthur J. Seaman, Robert D. Koler, Bernard Pirofsky
Rok vydání: 1960
Předmět:
Zdroj: The American Journal of Medicine. 29:857-864
ISSN: 0002-9343
DOI: 10.1016/0002-9343(60)90119-4
Popis: The studies of a forty-eight year old man who has a cryoglobulin with unique properties are presented herein. The cryoglobulin polymerizes to form a gel which interferes with the blood clotting test systems, causes increased blood viscosity, and slows peripheral circulation. The mechanism of these effects is related to hydrogen bond formation, which can be prevented in vivo and in vitro by basic organic amines. The protein has a long turnover time with a half-time of 18.8 days. It is related immunologically to gamma globulin but also has a specific immunologic reaction. Nitrogen balance studies showed a decrease in the concentration of cryoglobulin when the patient was in negative nitrogen balance. Removal of the abnormal protein by plasmapheresis resulted in lowering of the concentration from 9.5 to 4 to 5 gm. per cent and correction or improvement of all abnormal clinical and laboratory findings.
Databáze: OpenAIRE