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Abstract
The present studies demonstrate loss of human serum alpha-1 antitrypsin activity in
the presence of cultures of certain gram-negative bacterial organisms, as well as
by exposure to lyophilized culture supernate prepared from Pseudomonas aeruginosa. Antitrypsin inactivation was seen to develop within 11 hours after inoculation of
Pseudomonas aeruginosa into broth. Upon incubation of lyophilized antitrypsin inactivator (AI) with antitrypsin
at 37 °C., inactivation of antitrypsin increased as a function of time. Al was stable
at 56 °C. and at pH 5 through 8. Soybean trypsin inhibitor was not inactivated by
4 times the amount of AI required to inactivate an equivalent number of moles of alpha-1
antitrypsin. Identical peaks were eluted with Sephadex G-75 column chromatography
when AI and antitrypsin were fractionated separately or after prior preincubation,
supporting an enzymatic, rather than binding, action of AI on antitrypsin. AI may
play a role in inflammatory mechanisms involving human serum alpha-1 antitrypsin.
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Article info
Publication history
Accepted:
February 3,
1971
Received:
June 3,
1970
Footnotes
☆This work was supported by United States Public Health Service Grant AI-06849.
Identification
Copyright
© 1971 Published by Elsevier Inc.
