Extracellular metalloproteinase activity in Phytomonas françai.
Extracellular proteolytic activities were detected in Phytomonas françai culture supernatant. A 67-kDa enzyme was purified by ammonium sulfate precipitation and gel filtration in a HPLC system. This proteinase was optimally active at 28 degrees C and pH 5.0; and the use of proteolytic inhibitors indicated that it belongs to the metalloproteinase class. This is the first report on the purification of an extracellular metalloproteinase from a Phytomonas species.
Almeida
Flávia V S
FV
Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes, Universidade Federal do Rio de Janeiro, CCS Bloco I, 21941-590, Rio de Janeiro, Brazil.
Branquinha
Marta H
MH
Giovanni-De-Simone
Salvatore
S
Vermelho
Alane B
AB
D000818:Animals; D004492:Edetic Acid / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005109:Extracellular Matrix / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D020782:Matrix Metalloproteinases / Q000302:isolation & purification / Q000378:metabolism*; D010618:Phenanthrolines / Q000378:metabolism; D014351:Trypanosomatina / Q000145:classification / Q000201:enzymology*
D010618:Phenanthrolines; D004492:Edetic Acid; D020782:Matrix Metalloproteinases; C025205:1,10-phenanthroline