Dolhofer-Bliesener R, Gerbitz K D
Institut für Klinische Chemie, Städtisches Krankenhaus München Schwabing, FRG.
Scand J Clin Lab Invest. 1990 Nov;50(7):739-46. doi: 10.3109/00365519009091067.
Incubation of human immunoglobulin G (IgG) with glucose in vitro leads to the formation of glycated IgG concomitant with marked changes in functional properties of the Fc fragment. After 22 days of incubation in the absence and presence of 13.9, 27.7 and 55.5 mmol/l glucose, respectively, protein A binding was reduced by 42, 66 and 83%, depending on the glucose concentration employed. Binding of complement by IgG was abolished after incubation of the immunoglobulins for 13 days at 13.9 mmol/l glucose. In contrast, functional properties of the Fab region were unaffected upon glycation, as revealed by determination of antigen-binding capacity, antibody affinity and antibody concentration. The functional changes of the Fc fragment were observed at glycation levels comparable to those found in diabetics.
人免疫球蛋白G（IgG）与葡萄糖在体外孵育会导致糖化IgG的形成，同时Fc片段的功能特性会发生显著变化。分别在不存在葡萄糖以及存在13.9、27.7和55.5 mmol/l葡萄糖的情况下孵育22天后，蛋白A结合率分别降低了42%、66%和83%，这取决于所使用的葡萄糖浓度。在13.9 mmol/l葡萄糖中孵育免疫球蛋白13天后，IgG与补体的结合被消除。相比之下，通过测定抗原结合能力、抗体亲和力和抗体浓度发现，Fab区域的功能特性在糖化后未受影响。在与糖尿病患者中发现的糖化水平相当的情况下，观察到了Fc片段的功能变化。
