Polarization fluorescence studies on proteolytic activity of alpha 2-macroglobulin-trypsin complexes

When digestive enzymes are released into the blood, they may be completely inactivated by a variety of inhibitor present (alpha-1-protease inhibitor, antithrombin III, alpha 2-plasmin inhibitor, etc.) or only partially neutralized by alpha 2-macroglobulin. In this study, polarization fluorescence is used to demonstrate that complexes of alpha 2-macroglobulin with trypsin fluorescence is used to demonstrate that complexes of alpha 2-macroglobulin with trypsin can digest beta-endorphin, adrenocorticotropin, and beta-lipotropin. Furthermore, it has been shown that a small trypsin inhibitor (trasylol, mol. wt. 6500) can prevent this digestion, but that larger inhibitory proteins (i.e. soybean trypsin inhibitor, mol. wt. 21 500; alpha 1-protease inhibitor, mol. wt. 50 000) cannot.