Studies on the elastase-serum protein interaction. I. Molecular identity of the inhibitors in human serum and direct demonstration of inhibitor-elastase complexes by zone and immunoelectrophoresis

Baumstark, J.S.

Archives of Biochemistry and Biophysics 118(3): 619-630


ISSN/ISBN: 0003-9861
PMID: 4167390
DOI: 10.1016/0003-9861(67)90397-9
Accession: 025577637

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By impregnation of agar gel human whole serum electrophoretograms with elastase, followed by overlaying with specific substrate (elastin particles in agar), it has been shown that elastase inhibitors are present in both the 1- and 2-globulin fractions. Immunoelectrophoresis, at pH 8.6, of elastase-whole serum mixtures produced a single arc of precipitate only in the 1-globulin region when diffused against antibody specific for elastase. Electrophoretically isolated -globulin fractions (1 and 2) when reacted with elastase identified this protein inhibitor as a constituent of the 1-globulin fraction. It was subsequently identified as the 3.5S 1-glycoprotein (1- antitrypsin) of Schuitze when elastase-serum mixtures produced identical arcs of precipitate in the 1-globulin region (immunoelectrophoresis) with anti-1-glycoprotein or antielastase antibodies. The 2-globulin elastase inhibitor has been identified as the 2-macroglobulin. Electrophoretic mobilities of the inhibitors determined from the elastase-agar gel impregnation experiments (above) were found to be in excellent accord with values for these proteins published by other investigators. The 1-glycoprotein-elastase complex possessed an electrophoretic mobility roughly intermediate to that of the parent proteins, whereas the mobility of the 1-macroglobulinelastase complex was higher than that of either protein component.