Candiano G, Ghiggeri G M, Delfino G, Cavatorta F, Queirolo C
Clin Chim Acta. 1983 Feb 28;128(1):29-40. doi: 10.1016/0009-8981(83)90052-9.
A new procedure has been devised for the isolation of a glycosyl subunit of albumin from human serum. After the selective removal from serum proteins with affinity chromatography on Blue-Sepharose CL-6B, albumin was applied to a column of concanavalin-A Sepharose which resolved the protein in two subunits with different specific colour activity for carbohydrates, as tested with thiobarbituric acid assay. The glycosyl albumin bound to concanavalin-A Sepharose was homogeneous when examined by immunoelectrophoresis and sodium dodecyl-sulphate polyacrylamide electrophoresis, whereas it showed a microheterogeneity when tested by isoelectric focusing. The procedure was applied to a model system as well as to serum from normal and diabetic patients.
已设计出一种从人血清中分离白蛋白糖基亚基的新方法。在用蓝色琼脂糖凝胶CL - 6B进行亲和色谱从血清蛋白中选择性去除后，将白蛋白应用于伴刀豆球蛋白A琼脂糖柱，该柱将蛋白质分离为两个亚基，用硫代巴比妥酸测定法检测，这两个亚基对碳水化合物具有不同的比色活性。通过免疫电泳和十二烷基硫酸钠 - 聚丙烯酰胺电泳检测时，与伴刀豆球蛋白A琼脂糖结合的糖基化白蛋白是均一的，而通过等电聚焦检测时则显示出微不均一性。该方法应用于模型系统以及正常和糖尿病患者的血清。
