Biological and physical properties of a human m-cryoglobulin and its monomer subunit.

  • 1 December 1971
    • journal article
    • Vol. 9  (6) , 795-807
Abstract
A patient with Waldenstrom's macroglobulinaemia was found to have a serum cryoprecipitate which consisted entirely of a γMK-macroglobulin. This protein had no detectable antibody activity against a variety of other serum components and fixed only minimal amounts of complement over temperatures ranging from 4°C to 37°C. Precipitation of the cryoglobulin began at about 30°C and was complete at temperatures below 20°C. In contrast to other macroglobulins that have been reported, cryoprecipitability persisted after the protein was dissociated into its monomer subunits. Isolated subunits formed cryoprecipitates as did the hybrid macroglobulin formed from equal parts of such subunits and the subunits of a non-cryoprecipitating macroglobulin.