Harada K, Nakayama T, Kitamura M, Sugimoto T
Clin Chim Acta. 1975 Mar 24;59(3):291-9. doi: 10.1016/0009-8981(75)90004-2.
The characteristics of abnormally large-size amylase (macroamylase) of the three patients were studied. Amylase isoenzyme patterns of the three macroamylase samples of agar gel electrophoresis were different from the normal one: a post-beta-globulin or middle-ganna-globulin zone was found in macroamylase, while a fast-gamma, and a pre-gamma-globulin or both zones is found in normal amylase. With gel chromatography at pH 3.4, macroamylase dissociated to normalsized amylase. The electrophoretic patterns of the normal-sized amylase were identical with those of normal amylase. The binding proteins of the macroamylase were identified as immunoglobulin IgG in onecase and immunoglobulin IgA in the other two cases by the immunochemical criteria and immunoenzyme electropherogram. These immunoglobulins bound with serum amylase having normal molecular weight and electophoretic mobility to form macroamylase.
对三名患者异常大尺寸淀粉酶（巨淀粉酶）的特征进行了研究。这三个巨淀粉酶样品的琼脂凝胶电泳淀粉酶同工酶模式与正常模式不同：在巨淀粉酶中发现了β球蛋白后区或中γ球蛋白区，而在正常淀粉酶中发现了快速γ区以及前γ球蛋白区或两个区域。在pH 3.4条件下进行凝胶过滤时，巨淀粉酶解离为正常大小的淀粉酶。正常大小淀粉酶的电泳模式与正常淀粉酶的电泳模式相同。通过免疫化学标准和免疫酶电泳图谱，在一个病例中鉴定出巨淀粉酶的结合蛋白为免疫球蛋白IgG，在另外两个病例中为免疫球蛋白IgA。这些免疫球蛋白与具有正常分子量和电泳迁移率的血清淀粉酶结合形成巨淀粉酶。
