Sips H J, Claass A H, van Dongen J M, Willemsen R, Hoogeveen A T, Galjaard H, Sinaasappel M, Hauri H P, Sterchi E E
J Inherit Metab Dis. 1985;8(4):163-8. doi: 10.1007/BF01805427.
The intestinal microvillar enzyme complex sucrase-isomaltase has been studied in cystic fibrosis and control ileum. A number of biochemical parameters of the enzyme in ileum homogenates have been determined. Both solubilized as well as membrane-bound sucrase-isomaltase were analyzed with respect to their reaction with monoclonal antibodies against human sucrase-isomaltase. Finally the subcellular localization of sucrase-isomaltase was verified by immunoelectronmicroscopy or via the analysis of purified brush-border membrane preparations. At all levels no significant differences could be detected between sucrase-isomaltase of cystic fibrosis and control ileum. It is concluded that an abnormal subcellular localization and/or abnormal enzymatic activity of sucrase-isomaltase in cystic fibrosis intestine cannot explain the markedly decreased disaccharidase activities in amniotic fluids from pregnancies resulting in a child affected with cystic fibrosis.
已对囊性纤维化患者和对照回肠中的肠微绒毛酶复合物蔗糖酶-异麦芽糖酶进行了研究。测定了回肠匀浆中该酶的一些生化参数。针对抗人蔗糖酶-异麦芽糖酶的单克隆抗体，分析了可溶性以及膜结合的蔗糖酶-异麦芽糖酶与其反应情况。最后，通过免疫电子显微镜或对纯化的刷状缘膜制剂的分析，证实了蔗糖酶-异麦芽糖酶的亚细胞定位。在各个层面上，囊性纤维化患者的蔗糖酶-异麦芽糖酶与对照回肠之间均未检测到显著差异。得出的结论是，囊性纤维化肠道中蔗糖酶-异麦芽糖酶的亚细胞定位异常和/或酶活性异常，无法解释导致胎儿患囊性纤维化的妊娠羊水中二糖酶活性明显降低的原因。
