Neef L, Hütter H J, Böhme I, Dotschev D, Danev S T, Haschen R J
Enzyme. 1982;28(4):348-54. doi: 10.1159/000459122.
Using agarose gel electrophoresis, a faster moving alanine aminopeptidase (EC 3.4.11.2) has been demonstrated in the urine from cases of Fanconi syndrome, endemic (Balkan) nephropathy and advanced renal insufficiency. The enzyme was partially purified and its properties (isoelectric point, molecular weight, substrate specificity, influence of metal ions, Michaelis constant, antigenic behavior) were compared with those of normal kidney alanine aminopeptidase. Isoelectric points and antigenic properties are identical, but the molecular weights differ by a factor of about 2. Therefore, the greater electrophoretic mobility is due to the smaller size of the atypical enzyme.
利用琼脂糖凝胶电泳,已证实在范科尼综合征、地方性(巴尔干)肾病及晚期肾功能不全患者的尿液中,存在一种迁移速度更快的丙氨酸氨肽酶(EC 3.4.11.2)。该酶经部分纯化,并将其性质(等电点、分子量、底物特异性、金属离子的影响、米氏常数、抗原行为)与正常肾丙氨酸氨肽酶的性质进行了比较。等电点和抗原性质相同,但分子量相差约2倍。因此,非典型酶电泳迁移率更高是因其分子尺寸更小。