Nebinger P
Biol Chem Hoppe Seyler. 1986 Mar;367(3):161-7. doi: 10.1515/bchm3.1986.367.1.161.
Cell homogenate of Entamoeba histolytica trophozoites was investigated for amylolytic activity against various biogenic and synthetic substrates. After gel filtration of the cell homogenate on Sephadex G-150, six partly separated amylases (I to VI) differing in their substrate specificities were detected using maltose, amylose, amylopectin, 4-nitrophenyl alpha-glucoside and 4-nitrophenyl alpha-maltotetraoside. All enzymes are able to degrade amylose, amylopectin, glycogen and biogenic malto-oligosaccharides. Since amylase I and II, which accepted maltose as substrate, were found in fresh (cell-free) medium containing calf serum, the possibility cannot be excluded that these enzymes originate from the medium and therefore are not associated with E. histolytica trophozoites. Amylases III to VI, which were not found in fresh medium, were further purified by isoelectric focusing and chromatographic procedures using DEAE, CM ion exchange materials and Con A Sepharose 4B. pH, temperature optima and relative molecular masses were determined.
对溶组织内阿米巴滋养体的细胞匀浆进行了研究，以检测其对各种生物源和合成底物的淀粉酶活性。在Sephadex G - 150上对细胞匀浆进行凝胶过滤后，使用麦芽糖、直链淀粉、支链淀粉、4 - 硝基苯基α - 葡萄糖苷和4 - 硝基苯基α - 麦芽四糖检测到六种底物特异性不同的部分分离的淀粉酶（I至VI）。所有酶都能够降解直链淀粉、支链淀粉、糖原和生物源麦芽寡糖。由于在含有小牛血清的新鲜（无细胞）培养基中发现了以麦芽糖为底物的淀粉酶I和II，因此不能排除这些酶源自培养基，因而与溶组织内阿米巴滋养体无关的可能性。在新鲜培养基中未发现的淀粉酶III至VI，通过使用DEAE、CM离子交换材料和伴刀豆球蛋白A琼脂糖4B的等电聚焦和色谱程序进一步纯化。测定了pH、最适温度和相对分子质量。
