Characterization of proteinases in Herpetomonas anglusteri and Herpetomonas roitmani.
We have analyzed the proteinase profile of two Herpetomonas species, H. anglusteri and H. roitmani (a symbiont-bearing trypanosomatid), by in situ detection of enzyme activities on SDS-PAGE gels containing copolymerized gelatin as substrate. Two major cell-associated proteolytic activities, a 60 kDa zinc-metalloproteinase and a 45 kDa cysteine proteinase could be detected based on the inhibition of their activities by 1, 10-phenathroline and E-64, respectively. The trypanosomatids released into the growth medium distinct proteinases. H. anglusteri expressed three digestion haloes in the gels of approximately 60, 50, and 40 kDa, whereas H. roitmani secreted only a 60 kDa enzyme. However, these activities were inhibited by 1,10-phenanthroline, suggesting that all of them are zinc-metalloproteinase.
Souza dos Santos
A L
AL
Departamento de Microbiologia Geral, Instituto de Microbiologia Professor Paulo de Góes (IMPPG), CCS, Bloco I, Universidade Federal do Rio de Janeiro (UFRJ), Ilha do Fundão, 21941-590, Rio de Janeiro, RJ, Brasil.
Ferreira
A
A
Franco
V A
VA
Alviano
C S
CS
de Araújo Soares
R M
RM
D000818:Animals; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D014351:Trypanosomatina / Q000201:enzymology* / Q000254:growth & development; D015032:Zinc
D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases; D015032:Zinc