Extracellular metalloproteinases in Phytomonas serpens.
The detection of extracellular proteinases in Phytomonas serpens, a trypanosomatid isolated from tomato fruits, is demonstrated in this paper. Maximal production occurred at the end of the logarithmic phase of growth. These enzymes exhibited selective substrate utilization in SDS-PAGE, being more active with gelatin; hemoglobin and bovine serum albumin were not degraded. Three proteinases were detected in SDS-PAGE-gelatin, with apparent molecular masses between 94 and 70 kDa. The proteolytic activity was completely blocked by 1,10-phenanthroline and strongly inhibited by EDTA, whereas a partial inhibition was observed with trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) and soybean trypsin inhibitor; phenylmethylsulfonyl fluoride weakly inhibited the enzymes. This inhibition profile indicated that these extracellular proteinases belong to the metalloproteinase class.
Vermelho
Alane B
AB
Departamento de Microbiologia Geral, Instituto Microbiologia Prof. Paulo de Góes, Centro de Ciências de Saúde, Bl. I, Cidade Universitária, Universidade Federal do Rio de Janeiro, 21941-590, Rio de Janeiro, Brazil. abvermelho@micro.ufrj.br
Almeida
Flávia V S
FV
Bronzato
Leandro S
LS
Branquinha
Marta H
MH
D000818:Animals; D003470:Culture Media / Q000737:chemistry; D005110:Extracellular Space / Q000201:enzymology; D005780:Gelatin / Q000378:metabolism; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism; D014351:Trypanosomatina / Q000145:classification / Q000166:cytology / Q000201:enzymology* / Q000254:growth & development
D003470:Culture Media; D011480:Protease Inhibitors; D005780:Gelatin; D008666:Metalloendopeptidases