The Effect of Some Mercaptanes upon a Macro- Cryogelglobulin; Modifications Induced by Cysteamine, Penicillamine

Although macroglobulinemia of Waldenstr6m is a rare disorder, the physicochemical modification of macroglobulins therein has broad implications, since similar large proteins may be involved in the pathogenesis of symptoms associated with a variety of relatively common diseases; i.e., Rh isosensitization, hemolysis due to cold agglutinins, and so on. Also, a number of normally occurring proteins (properdin, isohemagglutinins, and others) are macroglobulins. In macroglobulinemia of Waldenstr6m the pathological proteins are responsible for the increased serum viscosity which is usually present (1). In certain instances the macroglobulins also possess the properties of cryoglobulins or cryogelglobulins, i.e., they precipitate or gel at temperatures lower than 370 C (2). These abnormal proteins (paraproteins) may be responsible for the production of Raynaud's phenomenon, ulcerations or gangrene. High environmental temperature may be somewhat helpful in preventing the damaging effects of cryo or cryogelglobulins. Plasmapheresis and exchange transfusions have not been found to be satisfactory in the elimination of the paraproteins over long periods of time (3, 4). Therefore, another avenue of investigation into phenomena related to these substances has been explored. Deutsch and Morton (5) and Glenchur, Zinneman and Briggs (6) have demonstrated that mercaptanes will depolymerize macroglobulins. The addition of 0.1 M cysteine at pH 7.4 to a macroglobulin with 18S, 25S and 32S components produced conversion to a single 6S component. Following removal of cysteine by dialysis, there was reaggregation of the proteins with the fornma-