Abstract
1. 1. A method for the isolation of crystalline macroglobulin from human serum is described. 2. 2. This protein behaves in electrophoresis as a monodisperse system. Its isoelectric point, computed from its mobility-pH curve, has been found at pH 6.4. 3. 3. The average value of D 20,w = 2.12 × 10 −7 has been obtained for its diffusion constant. 4. 4. The sedimentation diagram is characterized by the presence of three components with sedimentation constant values of S 20,w 0 = 15, S 20,w 0 = 34, and S 20,w 0 = 44.5 × 10 −13. 5. 5. The influence of acid, alkali, urea, guanidine, and detergent has been studied. 6. 6. Upon addition of mercaptoethanol, the macroglobulin dissociates into 6 S units, but it does not dissociate in the presence of other reducing agents. 7. 7. The average molecular weight of 1.28 × 10 6 has been calculated from lightscattering measurements, and intrinsic viscosity has been calculated as 0.19.
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