Abstract:
:Haemophilus paragallinarum secretes metalloproteases into different culture media lacking serum. Secreted proteins, concentrated by precipitation with 70% ammonium sulphate ((NH(4))(2)SO(4)) or methanol, displayed proteolytic activity at >100 kDa molecular mass in 10% polyacrylamide gels co-polymerized with porcine gelatin (0.1%). They were active in a broad pH range (4-9); pH 7.5 being the optimum. Protease activity was inhibited by 20 mmol EDTA/L and reactivated by calcium. The proteolytic activity was heat-stable at 40, 50, and 60 degrees C, but its activity diminished at 70 degrees C or higher. Secreted proteins partially degraded chicken immunoglobulin G (IgG) and cross-reacted with a polyclonal serum against a high molecular mass protease secreted by Actinobacillus pleuropneumoniae. Extracellular proteases could play a role in infectious coryza caused by H. paragallinarum.
journal_name
Can J Microbioljournal_title
Canadian journal of microbiologyauthors
Rivero-García PC,Cruz CV,Alonso PS,Vaca S,Negrete-Abascal Edoi
10.1139/w05-067subject
Has Abstractpub_date
2005-10-01 00:00:00pages
893-6issue
10eissn
0008-4166issn
1480-3275pii
w05-067journal_volume
51pub_type
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