The trypanocidal Cape buffalo serum protein is xanthine oxidase.
The trypanocidal Cape buffalo serum protein is xanthine oxidase.
复制标题
杀锥虫的非洲水牛血清蛋白是黄嘌呤氧化酶。
DOI：
10.1128/iai.65.9.3806-3814.1997
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发表时间：
1997
影响因子：
3.1
通讯作者：
Black,SJ
中科院分区：
文献类型：
--
作者：
Muranjan,M;Wang,Q;Li,YL;Hamilton,E;Otieno-Omondi,FP;Wang,J;VanPraagh,A;Grootenhuis,JG;Black,SJ
来自南非布法罗（Syncerus caffer）的血浆和血清在体外杀死所有种类的非洲锥虫的血流阶段。通过羟基磷灰石、蛋白A-G、Mono Q和Superose 12连续色谱法分离杀锥虫血清组分。纯化的杀锥虫蛋白的分子量为150 kDa，活性与还原十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后检测到的146 kDa多肽的存在相关。146-kDa还原多肽的三个肽片段的氨基酸序列、天然蛋白质的配体亲和性和免疫亲和层析以及对药理学抑制剂的敏感性，将杀锥虫物质鉴定为黄嘌呤氧化酶（EC 1.1.3.22）。杀锥虫活性导致锥虫糖酵解的抑制，是由于嘌呤分解代谢酶的细胞外黄嘌呤和次黄嘌呤的catalysis过程中产生的H2 O2。
Plasma and serum from Cape buffalo (Syncerus caffer) kill bloodstream stages of all species of African trypanosomes in vitro. The trypanocidal serum component was isolated by sequential chromatography on hydroxylapatite, protein A-G, Mono Q, and Superose 12. The purified trypanocidal protein had a molecular mass of 150 kDa, and activity correlated with the presence of a 146-kDa polypeptide detected upon reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid sequences of three peptide fragments of the 146-kDa reduced polypeptide, ligand affinity and immunoaffinity chromatography of the native protein, and sensitivity to pharmacological inhibitors, identified the trypanocidal material as xanthine oxidase (EC 1.1.3.22). Trypanocidal activity resulted in the inhibition of trypanosome glycolysis and was due to H2O2 produced during catabolism of extracellular xanthine and hypoxanthine by the purine catabolic enzyme.