Isolation and characterization of horse alpha 2-macroglobulin protease inhibitor.
Several publications have described in the past properties of partly purified horse alpha 2-macroglobulin (alpha 2M) which are strikingly different from the human alpha 2M. Horse alpha 2M was therefore isolated to purity by classical procedures, i.e. affinity chromatography, ion exchange chromatography and gel filtration, and its properties are compared with those of its human counterpart. The molecular weight of the native protein and its subunits, the isoelectrofocusing pattern and the change in electrophoretic mobility caused by interaction with protease were similar to those of human alpha 2M. Horse alpha 2M had a broad enzyme specificity and inhibited enzymatic action on macromolecules but not on small molecular weight synthetic substrates. In addition the horse and human alpha 2M were found to be immunochemically related when examined by specific antisera to human as well as to horse alpha 2-macroglobulin.
D000818:Animals; D006736:Horses / Q000097:blood*; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D013045:Species Specificity; D000511:alpha-Macroglobulins / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*
D046911:Macromolecular Substances; D011480:Protease Inhibitors; D000511:alpha-Macroglobulins