Advertisement

Bacterial inactivation of human serum alpha-1 antitrypsin

      This paper is only available as a PDF. To read, Please Download here.

      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.
      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Translational Research
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect

      References

        • Talamo R.C.
        • Allen J.D.
        • Kahan M.G.
        • Austen K.F.
        Hereditary alpha-1-antitrypsin deficiency.
        New Eng. J. Med. 1968; 278: 345
        • Welch M.H.
        • Reinecke M.E.
        • Hammarsten J.F.
        • Guenter C.A.
        Antitrypsin deficiency in pulmonary disease: The significance of intermediate levels.
        Ann. Intern. Med. 1969; 71: 533
        • Eisen A.F.
        • Bloch K.J.
        • Sakai T.
        Inhibition of human skin collagenase by human serum.
        J. Lab. Clin. Med. 1970; 75: 258
        • Troyer H.
        • Moskowitz R.W.
        Serum trypsin inhibitor: A comparison of assay methods using amide and casein substrates.
        Enzym. Biol. Clin. 1968; 9: 1
        • Erlanger B.F.
        • Kokowsky N.
        • Cohen W.
        The preparation and properties of two new chromogenic substrates of trypsin.
        Arch. Biochem. 1961; 95: 271
        • Wieme R.J.
        Agar-gel electrophoresis.
        in: Elsevier Publishing Company, Amsterdam1965: 195
        • Altemeier W.A.
        • Wulsin J.
        • Culbertson W.R.
        • MacMillan B.
        • Yale C.
        • Cole W.
        • Vetto M.
        Exotoxin aspects of shock.
        in: Fed. Proc. 20. 1961: 173 (Suppl. 9)
        • Rimon A.
        • Shamash Y.
        • Shapiro B.
        The plasmin inhibitor of human plasma.
        J. Biol. Chem. 1966; 241: 5102
        • Kueppers F.
        • Bearn A.G.
        A possible experimental approach to the association of hereditary alpha-1 antitrypsin deficiency and pulmonary emphysema.
        in: Proc. Soc. Exp. Biol. Med. 121. 1966: 1207