PMID: 6171538Oct 1, 1981Paper

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

International Journal of Peptide and Protein Research
L Karic, C B Glaser

Abstract

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.

References

Aug 15, 1978·Analytical Biochemistry·G D VircaR C Roberts
Jul 9, 1975·Clinica Chimica Acta; International Journal of Clinical Chemistry·J F MeyerP Metais
Sep 1, 1973·The Journal of Clinical Investigation·P C Harpel, M W Mosesson
May 1, 1970·Clinica Chimica Acta; International Journal of Clinical Chemistry·H RinderknechtB J Haverback
Jan 22, 1981·Clinica Chimica Acta; International Journal of Clinical Chemistry·J Hermon-TaylorJ Dunham
Oct 14, 1980·Biochemistry·J W BrodrickH Maeda
Nov 30, 1967·Biochemical and Biophysical Research Communications·T Chase, E Shaw

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