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The interaction of horse alpha 2-macroglobulin with methylamine, trypsin and cathepsin D was studied by circular dichroism in the far and near UV region, by polyacrylamide gel electrophoresis and by determination of its inhibitory activity. The CD spectra of horse alpha 2-macroglobulin resemble those of bovine und human alpha 2-macroglobulin. The CD spectra were changed in a different manner after the interaction of alpha 2-macroglobulin with methylamine, trypsin and inactive or active cathepsin D, indicating that more than one conformational change occurs. Cathepsin D activity was not affected by complex formation with horse alpha 2-macroglobulin. In contrast to the action of trypsin, treatment with methylamine did not increase the electrophoretic mobility of alpha 2-macroglobulin.

Horse α 2 -Macroglobulin. Circular Dichroism Studies of Conformational Changes upon Reaction with Proteinases and Methylamine