title: Chitinolytic activities in Trichomonas vaginalis.
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.
authors.affiliation: Biologie et Contrôle des Organismes Parasites, Faculté de Pharmacie, Université de Paris-Sud, Châtenay-Malabry.
authors.forename: A
authors.initials: A
authors.lastname: Sanon
authors.forename: C
authors.initials: C
authors.lastname: Bories
authors.forename: P M
authors.initials: PM
authors.lastname: Loiseau
mesh_terms: D000818:Animals; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000378:metabolism*; D003470:Culture Media; D005260:Female; D006596:Hexosaminidases / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000032:analysis; D008291:Malate Dehydrogenase / Q000032:analysis; D014247:Trichomonas Vaginitis / Q000469:parasitology; D014246:Trichomonas vaginalis / Q000201:enzymology*; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism
chemical_list: D003470:Culture Media; D002686:Chitin; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; C079639:1,4-beta-chitobiosidase; D006596:Hexosaminidases; C086400:chitotriosidase; D002688:Chitinases; D001619:beta-N-Acetylhexosaminidases