Isolation of active subforms of alpha 2-macroglobulin

Anion-exchange chromatography is shown to permit resolution and separation of subforms of the serum glycoprotein alpha 2-macroglobulin. The subforms differ dramatically in their stability as judged by differential scanning calorimetry, undergoing thermally induced unfolding at temperatures of 61 and 69 degrees C respectively. In addition, the proteinase-binding stoichiometry of the subforms differs by a factor of 2, with the more- and less-stable forms binding 2 and 1 mol of proteinase per mol of tetramer respectively. The calorimetric stability of the two forms is differentially affected on treatment with neuraminidase, suggesting that the nature of glycosylation may in part account for the observed differences in physical and functional properties.