1987•Clinical Chemistry and Laboratory Medicine (CCLM)Open access

Determination of Functional Activity of α1-Protease Inhibitor and α2-Maeroglobulin in Human Plasma Using Elastase

M C Gaillard, Terence Arthur Kilroe-Smith

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Abstract

The competitive binding of human alpha 1-antitrypsin and human alpha 2-macroglobulin to porcine pancreatic elastase was studied. Mixtures of these two protease inhibitors, when titrated against elastase give inhibition curves analogous to those obtained with human plasma. This is however not the case when the individual inhibitors are used. A theoretical treatment enabled us to devise an assay method to determine the amounts of functional activity of alpha 1-protease inhibitor and alpha 2-macroglobulin respectively in human plasma.

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The competitive binding of human alpha 1-antitrypsin and human alpha 2-macroglobulin to porcine pancreatic elastase was studied. Mixtures of these two protease inhibitors, when titrated against elastase give inhibition curves analogous to those obtained with human plasma. This is however not the case when the individual inhibitors are used. A theoretical treatment enabled us to devise an assay method to determine the amounts of functional activity of alpha 1-protease inhibitor and alpha 2-macroglobulin respectively in human plasma.

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Available abstract

The competitive binding of human alpha 1-antitrypsin and human alpha 2-macroglobulin to porcine pancreatic elastase was studied. Mixtures of these two protease inhibitors, when titrated against elastase give inhibition curves analogous to those obtained with human plasma. This is however not the case when the individual inhibitors are used. A theoretical treatment enabled us to devise an assay method to determine the amounts of functional activity of alpha 1-protease inhibitor and alpha 2-macroglobulin respectively in human plasma.

Key concepts: Elastase, alpha-2-Macroglobulin, Human plasma, Pancreatic elastase, Protease, Protease inhibitor (pharmacology), Alpha (finance), Chemistry

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