文章基本信息

标题：Secreted acid phosphatase of Leishmania mexicana: a filamentous phosphoglycoprotein polymer
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作者：T Ilg ; Y D Stierhof ; R Etges 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1991
卷号：88
期号：19
页码：8774-8778
DOI：10.1073/pnas.88.19.8774
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：In the promastigote, or insect stage, most species of the parasitic protozoan Leishmania secrete an acid phosphatase. The enzyme purified from the culture medium of Leishmania mexicana is shown to be a complex [13.3% (wt/wt) protein, 74.4% (wt/wt) carbohydrate, and 12.3% (wt/wt) phosphate] composed of a predominant phosphorylated glycoprotein with a relative molecular mass of 100 kDa and noncovalently associated high molecular mass (proteo)phosphoglycans. Electron microscopy discloses long filaments composed of a central chain of protein subunits surrounded by a diffuse glycocalix that can be decorated by monoclonal antibodies or concanavalin A. In contrast to the polymeric structure of the L. mexicana enzyme, the acid phosphatase secreted by Leishmania donovani is mono- or oligomeric but not filamentous.