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The present study indicates that crystalline elastase of Pseudomonas aeruginosa is a very potent inactivator of human plasma alpha 1-proteinase inhibitor, the enzyme (E) inactivated the inhibitor (I) almost completely within 1 h at 25 degrees C at a molar ratio of E/I = 1:100. The crystalline P. aeruginosa protease also inactivated the inhibitor, but 100-fold less. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the alpha 1-proteinase inhibitor inactivated by the elastase and protease showed decreases in molecular weight of approximately 5,000 and 10,000, respectively. Regeneration of trypsin was negligible even when bovine trypsin-alpha 1-proteinase inhibitor complex (E/I = 1.0) was treated with the elastase. The affinity of alpha 1-proteinase inhibitor to trypsin was much higher than that to elastase. It was suggested that, assuming the pseudomonal proteases are produced and can inactivate alpha 1-proteinase inhibitor in vivo during pseudomonal diseases, the loss of alpha 1-proteinase inhibitor activity may permit the endogenous serine proteases to cause tissue destruction.
K Morihara, and
H Tsuzuki, and
K Oda
August 1984,
Biochimica et biophysica acta,
K Morihara, and
H Tsuzuki, and
K Oda
December 1982,
The American review of respiratory disease,
K Morihara, and
H Tsuzuki, and
K Oda
December 1989,
Infection and immunity,
K Morihara, and
H Tsuzuki, and
K Oda
September 1992,
The Journal of infectious diseases,
K Morihara, and
H Tsuzuki, and
K Oda
April 1993,
Biochimica et biophysica acta,
K Morihara, and
H Tsuzuki, and
K Oda
September 1981,
Biochemical and biophysical research communications,
K Morihara, and
H Tsuzuki, and
K Oda
February 1991,
Annals of the rheumatic diseases,
K Morihara, and
H Tsuzuki, and
K Oda
June 1980,
The American review of respiratory disease,
K Morihara, and
H Tsuzuki, and
K Oda
April 1990,
FEBS letters,
K Morihara, and
H Tsuzuki, and
K Oda
March 1987,
The American review of respiratory disease,
