Kinetic and Chemical Evidence for the Inability of Oxidized α1-Proteinase Inhibitor to Protect Lung Elastin from Elastolytic Degradation
K BEATTY, N MATHESON, J TRAVIS - 1984 - degruyter.com
K BEATTY, N MATHESON, J TRAVIS
1984•degruyter.comThe oxidation of human al-proteinase inhibitor results in the conversion of this protein into a
form which cannot protect lung elastin from degradation by elastolytic proteinases. Data
indicate that this is primarily because of the lowering of the association rate between the
modified inhibitor and neutrophil elastase, as well as in a change inK {from near 10~ 14 to
near 10~ 10M. This is consistent with the hypothesis that oxidation of!-proteinase inhibitor in
the lung by cigarette smoke results in a lowering of the protection of this organ from …
form which cannot protect lung elastin from degradation by elastolytic proteinases. Data
indicate that this is primarily because of the lowering of the association rate between the
modified inhibitor and neutrophil elastase, as well as in a change inK {from near 10~ 14 to
near 10~ 10M. This is consistent with the hypothesis that oxidation of!-proteinase inhibitor in
the lung by cigarette smoke results in a lowering of the protection of this organ from …
Summary
The oxidation of human al-proteinase inhibitor results in the conversion of this protein into a form which cannot protect lung elastin from degradation by elastolytic proteinases. Data indicate that this is primarily because of the lowering of the association rate between the modified inhibitor and neutrophil elastase, as well as in a change inK {from near 10~ 14 to near 10~ 10M. This is consistent with the hypothesis that oxidation of!-proteinase inhibitor in the lung by cigarette smoke results in a lowering of the protection of this organ from elastolytic degradation.
De Gruyter