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J. Biol. Chem., Vol. 255, Issue 9, 3931-3934, May, 1980
K Beatty, J Bieth and J Travis
The association rate constants for the interaction of alpha-1- proteinase
inhibitor, oxidized alpha-1-proteinase inhibitor, and alpha-
1-antichymotrypsin with several mammalian serine proteinases have been
determined. The results indicate that leukocyte elastase reacts more
rapidly with alpha-1-proteinase inhibitor than any other proteinase tested,
while leukocyte cathepsin G shows the strongest association with
alpha-1-antichymotrypsin. Oxidation of the critical methionine residue of
alpha-1-proteinase inhibitor reduces the association with leukocyte
elastase by a factor of more than 2000 and also lowers the association with
all of the other enzymes tested with the exception of chymotrypsin.
Significantly, oxidation completely abolishes any interaction of
alpha-1-proteinase inhibitor with porcine elastase, human plasmin or human
thrombin. These data support previous results (Johnson, D., and Travis, J.
(1979) J. Biol. Chem. 254, 4022-4026) which indicated that oxidation of
human alpha-1-proteinase inhibitor in vivo could reduce the effectiveness
of this inhibitor in controlling proteolysis. In the lung, in particular,
oxidizing agents of both chemical and biological sources could, indirectly,
augment elastolysis in this tissue, resulting in the development of
pulmonary emphysema.
Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin
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