VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

The effect of Legionella pneumophila metalloproteinase on certain human blood proteins. Cleavage of anti(1)-antitrypsin and acid-stable serine proteinase inhibitors

   
Gul'nik S.V., Feokharus G., Varchenko N.V., Lavrenova G.I., Stepanov V.M.
PubMed Id: 1949672
Year: 1991  Volume: 37  Issue: 3  Pages: 14-17
Antitryptic activity of human blood serum was decreased after incubation with metalloproteinase from Legionella pneumophila. The enzymatic activity depends on the time of incubation as well as on the ratio between the enzyme content and blood serum total protein. Cross immunoelectrophoresis, involving monospecific rabbit antiserum towards the alpha 1-antitrypsin, demonstrated highly effective hydrolysis of alpha 1-antitrypsin by the metalloproteinase. As shown by polyacrylamide gel electrophoresis the metalloproteinase hydrolyzed acid stable inhibitor of serine proteinases into fragments with distinct loss of the inhibitor activity. Thermolysine hydrolyzed similarly the proteins studied but at a lower rate. The metalloproteinase from L. pneumophila appears to be mainly responsible for production of utilizable components from protein substrates involved in vital activity of the bacteria. It may not be excluded that the enzyme is able to impair some host protective mechanisms.
Download PDF:
Reference:

Gul'nik S.V., Feokharus G., Varchenko N.V., Lavrenova G.I., Stepanov V.M. (1991) Voprosy meditsinskoi khimii, 37(3), 14-17.
References
 2002 (vol 48)
 2001 (vol 47)
 2000 (vol 46)
 1999 (vol 45)
 1998 (vol 44)
 1997 (vol 43)
 1996 (vol 42)
 1995 (vol 41)
 1994 (vol 40)
 1993 (vol 39)
 1992 (vol 38)
 1991 (vol 37)
 1990 (vol 36)
 1989 (vol 35)
 1988 (vol 34)
 1987 (vol 33)