The Effect of Leucocyte Elastase on the Immunoelectrophoretic Behaviour of α1-Antitrypsin

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Abstract
Two-dimensional immunoelectrophoresis and conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed on various mixtures of purified .alpha.1-antitrypsin (.alpha.1AT) and leukocyte elastase (LE). Results confirm that .alpha.1AT inhibits LE by the formation of enzyme-inhibitor complexes demonstrable by both techniques. The complexes break down with time and are not affected by pH in the presence of excess .alpha.1AT. The breakdown is more rapid in the presence of excess enzyme only at pH values where LE remains active. The resultant products of the complex breakdown include inactivated LE and .alpha.1AT that has undergone limited proteolysis. Presence or absence of .alpha.1AT-enzyme complexes as demonstrated by 2-dimensional immunoelectrophoresis must be interpreted with caution when studying .alpha.1AT function in lung secretions. The absence of such complexes does not mean that previous interaction with enzyme has not occurred, thereby accounting for a reduction in .alpha.1AT inhibitory capacity.

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