Identification and characterization of an alpha-mannosidase from Trypanosoma cruzi.
Identification and characterization of an alpha-mannosidase from Trypanosoma cruzi.
复制标题
克氏锥虫 α-甘露糖苷酶的鉴定和表征。
DOI：
10.1093/glycob/2.6.563
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发表时间：
1992
期刊：
影响因子：
4.3
通讯作者：
Oeltmann,TN
中科院分区：
文献类型：
--
作者：
Swanson,PM;Carter,CE;Hager,C;Kim,WJ;Obermeier,S;Oeltmann,TN
在本报告中，我们描述了来自人类寄生虫克氏锥虫的酸性 α-甘露糖苷酶的首次纯化和表征。纯化的酶表现出天然摩尔。重量为 240 000 Da，显然由四个相同的摩尔亚基组成。重量 58 000 Da。四个亚基中的每一个都含有一个N-连接的高甘露糖型寡糖。 α-甘露糖苷酶的最适 pH 值为 3.5，pI 为 5.9。这种低 pH 最适值和苦马豆素抑制其活性的能力表明 α-甘露糖苷酶是一种溶酶体酶。针对T.cruzi酶的抗体不与哺乳动物溶酶体α-甘露糖苷酶反应，相反，针对大鼠溶酶体α-甘露糖苷酶的抗体不与T.cruzi酶反应。因此，T.cruzienzyme 似乎与其哺乳动物对应物不同。
In this report we describe the first purification and characterization of the acid α-mannosidase from the human parasiteTrypanosoma cruzi. The purified enzyme exhibited a native mol. wt of 240 000 Da and is apparently composed of four identical subunits of mol. wt 58 000 Da. Each of the four subunits contains one N-linked high-mannose-type oligosaccharide. The α-mannosidase exhibited a pH optimum of 3.5 and a pI of 5.9. This low pH optimum and the ability of swainsonine to inhibit its activity suggest that the α-mannosidase is a lysosomal enzyme. Antibodies against theT.cruzienzyme did not react with mammalian lysosomal α-mannosidase and, conversely, antibody against a rat lysosomal α-mannosidase did not react with theT.cruzienzyme. Thus, theT.cruzienzyme appears to be distinct from its mammalian counterpart.