Bacterial inactivation of human serum alpha-1 antitrypsin

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      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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