Extracellular dephosphorylation in the parasite, leishmania major / Desfosforilacion extracelular en el parasito, leishmania major
Acta cient. venez
;
42(6): 326-9, 1991. ilus, tab
Artículo
en Inglés
| LILACS
| ID: lil-105916
RESUMO
Leishmania major promastigotes were analyzed for the presence of protein phosphatase activity in intact cells and membrane-enriched fractions. Parasite phosphoprorylated in live cells with {*-32P} adenosine 5'-triphosphate (ATP) and an edogemous leishmanial ectokinase, were dephosphorylated by endogenous protein phosphatase like activity in intact cells and membrane-rich fractions. An alkaline phosphatase-like activity was also identified using the artificial substrate, p-nitrophenyl phosphate (pNPP). This activity was localized on the extracellular membrane of intact parasite, as well as in the particulate fraction of lysed cells. The phosphatase activity measure using pNPP had inhibition properties and a pH profile between protein phosphatases and general alkaline phosphatase. This study supports the observation that there is extracellular protein phosphorylation/dephosphorylation in L.major which may play a significant role in host-cell-parasite recognition and infection
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Índice:
LILACS (Américas)
Asunto principal:
Leishmania tropica
/
Fosfoproteínas Fosfatasas
/
Fosfatasa Alcalina
Tipo de estudio:
Estudio pronóstico
Idioma:
Inglés
Revista:
Acta cient. venez
Asunto de la revista:
Ciencia
Año:
1991
Tipo del documento:
Artículo
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