Koyama I, Sakagishi Y, Komoda T
J Chromatogr. 1986 Jan 10;374(1):51-9. doi: 10.1016/s0378-4347(00)83252-1.
Differences among rat alkaline phosphatases from various organs were established by using the serial lectin affinity technique. Elution profiles of isozymes with various lectin columns were significantly different from each other, and it was possible to distinguish between isozymes by this technique. It has been shown by many workers that a high-mannose-type and/or hybrid-type sugar chain is contained in the fraction bound strongly to concanavalin A-Sepharose. The duodenal alkaline phosphatase had a low content of this fraction, although the content of this fraction obtained from duodenal explants was increased markedly when explants were cultured with swainsonine, which is an inhibitor of alpha-mannosidase II, and this leads to the accumulation of high-mannose-type and hybrid-type sugar chains in the pathway of sugar chain processing. From the present results, it is suggested that differences in the elution profiles of isozymes may be due to the structural differences of sugar chains in alkaline phosphatases.
利用连续凝集素亲和技术确定了来自大鼠不同器官的碱性磷酸酶之间的差异。不同凝集素柱上同工酶的洗脱图谱彼此显著不同，通过该技术可以区分同工酶。许多研究人员已经表明，与伴刀豆球蛋白A-琼脂糖强烈结合的部分含有高甘露糖型和/或杂合型糖链。十二指肠碱性磷酸酶中该部分的含量较低，然而，当用α-甘露糖苷酶II抑制剂苦马豆素培养十二指肠外植体时，从十二指肠外植体获得的该部分含量显著增加，这导致糖链加工途径中高甘露糖型和杂合型糖链的积累。根据目前的结果，推测同工酶洗脱图谱的差异可能是由于碱性磷酸酶中糖链的结构差异所致。
