James G T, Austin J H
Clin Chim Acta. 1979 Oct 15;98(1-2):103-11. doi: 10.1016/0009-8981(79)90170-0.
Arylsulfatase A was purified to apparent homogeneity from normal human livers obtained at autopsy. According to gel electrophoresis in sodium dodecyl sulfate, purified arylsulfatase A consistently contained two subunits of slightly different sizes: approximately 69 000 and 57 000 daltons, but were not present in stoichiometrically equal amounts. Peptide maps of the entire enzyme and of the two individual subunits showed that the two polypeptides share similar if not identical sequences. These observations raise the possibility that the smaller polypeptide might be derived from the larger one. The sensitive peptide mapping procedures employed will make feasible future studies with the abnormal enzyme found in metachromatic leukodystrophy.
芳基硫酸酯酶A从尸检获得的正常人肝脏中纯化至表观均一。根据十二烷基硫酸钠中的凝胶电泳，纯化的芳基硫酸酯酶A始终含有两个大小略有不同的亚基：约69000和57000道尔顿，但化学计量比并不相等。整个酶以及两个单独亚基的肽图显示，这两种多肽即使序列不完全相同，也具有相似性。这些观察结果增加了较小多肽可能源自较大多肽的可能性。所采用的灵敏肽图分析方法将使未来对异染性脑白质营养不良中发现的异常酶的研究变得可行。
