Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity.
Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity.
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正常人肺和肺肿瘤中的芳基硫酸酯酶 a 表现出不同模式的微观异质性。
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发表时间：
1984
期刊：
影响因子：
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通讯作者：
A. Makita
中科院分区：
文献类型：
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作者：
M. Nakamura;S. Gasa;A. Makita
在十二烷基硫酸钠存在下，经电泳测定，从人肺中纯化出芳基硫酸酯酶A具有明显的均匀性。等电聚焦检查时，正常肺和肺腺癌的酶表现出相当大的微观异质性，等电点（pI）在5.1至4.6之间。与正常肺酶相比，肿瘤酶具有更多的异质性和酸性成分。通过外源水解酶处理，研究了电荷不均匀性的原因。在唾液酸酶、磷酸酶或内- β - n -乙酰氨基葡萄糖酶H（内糖苷酶H）处理后，等电聚焦凝胶上的酸性酶形态转移到碱性区域。将芳基磺化酶A与内糖苷酶H和唾液酸酶联合处理后，大部分酸性成分完全丧失，只剩下酸性较弱的成分，其pI分别为5.1、5.0和4.9。这些结果强烈表明，芳香基磺化酶A的电荷异质性不仅是由于唾液化，而且是由于酶的碳水化合物部分的磷酸化，并且在肿瘤酶中酸性基团的取代程度显着增加。
Arylsulfatase A was purified from human lung to apparent homogeneity as determined by electrophoresis in the presence of sodium dodecyl sulfate. The enzyme from normal lung as well as that from lung adenocarcinoma showed considerable microheterogeneity when examined by isoelectric focussing, with an isoelectric point (pI) ranging from 5.1 to 4.6. The tumor enzyme was more heterogeneous and contained more acidic components than the normal lung enzyme. The cause of the charge heterogeneity was examined by treatment with exogenous hydrolases. Upon treatment with sialidase, phosphatase or endo-beta-N-acetylglucosaminidase H (endoglycosidase H), the acidic enzyme forms shifted to an alkaline region on isoelectric focussing gels. Combined treatment of the arylsulfatase A with endoglycosidase H and sialidase resulted in complete loss of the most acidic components to give the less acidic components with pI 5.1, 5.0, and 4.9. These results strongly suggest that the charge heterogeneity of arylsulfatase A is due not only to sialylation but also to phosphorylation at the carbohydrate moiety of the enzyme, and the extent of substitution by acidic groups is markedly increased in the tumor enzyme.