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.
D000324:Adrenocorticotropic Hormone / Q000378:metabolism; D004723:Endorphins / Q000378:metabolism; D005454:Fluorescence Polarization; D014357:Trypsin / Q000378:metabolism*; D000511:alpha-Macroglobulins / Q000378:metabolism*; D001615:beta-Endorphin; D008083:beta-Lipotropin / Q000378:metabolism
D004723:Endorphins; D000511:alpha-Macroglobulins; D001615:beta-Endorphin; D000324:Adrenocorticotropic Hormone; D008083:beta-Lipotropin; D014357:Trypsin