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The separation of alpha-2 macroglobulin into five components with differing electrophoretic and enzyme-binding properties
Russell Saunders, … , Wilton E. Vannier, Bernard J. Haverback
Russell Saunders, … , Wilton E. Vannier, Bernard J. Haverback
Published November 1, 1971
Citation Information: J Clin Invest. 1971;50(11):2376-2383. https://doi.org/10.1172/JCI106736.
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Research Article

The separation of alpha-2 macroglobulin into five components with differing electrophoretic and enzyme-binding properties

Abstract

The alpha-2 macroglobulins from human serum and plasma were isolated by Bio-Gel P-300 and A5m gel filtration. The material showed a single peak on sedimentation velocity ultracentrifugation, a mol wt of 650,000 by sedimentation equilibrium ultracentrifugation, and a major precipitin arc in the alpha-2 macroglobulin region by immunoelectrophoresis against whole human serum. Two bands were observed in the alpha-2 macroglobulin region when acrylamide gel electrophoresis was performed with a pH 8.9 running gel. When a pH 7.8 gel was used, five electrophoretic species were observed. In both cases, the preaddition of stoichiometric amounts of trypsin or chymotrypsin added to alpha-2 macroglobulin resulted in disappearance of slower bands leaving only one band on acrylamide gel electrophoresis patterns.

Authors

Russell Saunders, Barbara J. Dyce, Wilton E. Vannier, Bernard J. Haverback

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