Surface antigens of Leishmania donovani promastigotes.
نویسندگان
چکیده
منابع مشابه
Surface antigens of Leishmania donovani promastigotes
Surface antigen profiles of Leishmania donovani promastigote isolates have been studied. Surface patterns of Brazilian and African isolates display remarkable similarities and are extremely simple, consisting of three major peptides of 65,000, 25,000, and 23,000 mol wt. Surface iodination and biosynthetic labeling coupled to immunoprecipitation techniques revealed that a single major determinan...
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Leishmania donovani, the agent of visceral leishmaniasis , is a t r y p a n o s o m a t i d protozoan t r ansmi t t ed by ph leboto in ine sandflies. The paras i te cycles between a nonmot i le , in t race l lu la r amast igote stage paras i t iz ing the mononuc lea r phagocytes of the mammal ian host and an extracel lular , moti le p romas t igo te stage in the insect vector, A s imilar p roma...
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The genome sequencing of several Leishmania species has provided immense amounts of data and allowed the prediction of the metabolic pathways potentially operating. Subsequent genetic and proteomic studies have identified stage-specific proteins and putative virulence factors but many aspects of the metabolic adaptations of Leishmania remain to be elucidated. In this study, we have used an unta...
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Amphotericin B (AmB)-resistant Leishmania donovani promastigotes were selected by increasing drug pressure, and their biological features were compared with those of the wild-type parent strain. The 50% inhibitory concentration for resistant cells was 20 times higher than that for the wild-type. Resistance was stable after more than 40 passages in drug-free medium, and resistant promastigotes w...
متن کاملIdentification of a surface membrane proton-translocating ATPase in promastigotes of the parasitic protozoan Leishmania donovani.
ATPase activities were measured in surface membranes and mitochondria isolated from promastigotes of the parasitic protozoan Leishmania donovani. The two enzymes were differentiated on the basis of pH optima, inhibitor sensitivity and by immunochemical methods. The surface-membrane (SM-) ATPase had an activity of 100 nmol/min per mg of protein, which was optimal at pH 6.5. The enzyme was Mg2+-d...
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ژورنال
عنوان ژورنال: Journal of Experimental Medicine
سال: 1983
ISSN: 0022-1007,1540-9538
DOI: 10.1084/jem.157.5.1562