Chitinolytic activities in Trichomonas vaginalis

Parasite. 1998 Mar;5(1):75-8. doi: 10.1051/parasite/1998051075.

Abstract

Chitinolytic activities were identified in the Protozoa Trichomonas vaginalis. Overall chitinase activity assessed using chitine-azure as substrate was 10.93 +/- 1.21 nmoles/min/mg prot. End nonreducing chitobiosidase (exochitinase) and chitotriosidase (endochitinase) activities were shown using p-nitrophenyl-substrates and had specific activities of 4.55 +/- 0.53 and 0.47 +/- 0.06 nmol/min/mg prot, Kmapp. = 1.32 mM and 5 microM and pH optimum = 7.0 and 6.1 respectively. beta-N-acetylhexosaminidase (NAHase) activity was also detected with a specific activity of 5.40 +/- 0.65 nmol/min/mg prot., Kmapp = 0.656 mM and pH optimum at 7.0. No release of these enzymes into the culture medium was found. The possible role of chitinases in T. vaginalis remains to be investigated.

MeSH terms

  • Animals
  • Chitin / metabolism
  • Chitinases / metabolism*
  • Culture Media
  • Female
  • Hexosaminidases / metabolism
  • Hot Temperature
  • Humans
  • Hydrogen-Ion Concentration
  • L-Lactate Dehydrogenase / analysis
  • Malate Dehydrogenase / analysis
  • Trichomonas Vaginitis / parasitology
  • Trichomonas vaginalis / enzymology*
  • beta-N-Acetylhexosaminidases / metabolism

Substances

  • Culture Media
  • Chitin
  • L-Lactate Dehydrogenase
  • Malate Dehydrogenase
  • 1,4-beta-chitobiosidase
  • Hexosaminidases
  • chitotriosidase
  • Chitinases
  • beta-N-Acetylhexosaminidases