Neu J, Crim W N, Sadowski J A
Enzyme. 1984;32(3):133-41. doi: 10.1159/000469466.
Comparisons between papain- and Triton X-100-solubilized lactase (EC 3.2.1.23) were made in terms of elution from various chromatographic columns and by molecular weight determinations. Using these techniques, no major differences could be detected. Since papain-solubilized enzyme would be cleaved at the hydrophilic-hydrophobic interface and detergent would release the amphipathic enzyme, the lack of detectable differences between purified lactase solubilized by the two agents suggests the existence of a relatively small anchoring moiety in rats when compared to that suggested in previous studies for adult humans.
就从各种色谱柱上的洗脱情况以及分子量测定而言,对木瓜蛋白酶和 Triton X - 100 增溶的乳糖酶(EC 3.2.1.23)进行了比较。使用这些技术,未检测到重大差异。由于木瓜蛋白酶增溶的酶会在亲水 - 疏水界面处裂解,而去污剂会释放两亲性酶,与先前对成年人类的研究相比,这两种试剂增溶的纯化乳糖酶之间缺乏可检测到的差异表明大鼠体内存在相对较小的锚定部分。