Schleicher E D, Mayer R, Wagner E M, Gerbitz K D
Klin. Chem. Institut, Krankenhaus Schwabing, München, F.R.G.
Clin Chem. 1988 Feb;34(2):320-3.
We compared the fructosamine activity in sera from healthy and diabetic subjects with the degree of protein glycation detected by a liquid-chromatographic method. The latter technique measures furosine as a specific product after hydrolysis of epsilon-amino-fructose-lysine. Our results indicate that the fructosamine assay measures the extent of glycation of purified human serum albumin correctly. On the other hand, we found no correlation between the two methods for sera from healthy subjects, although for diabetics' sera the values obtained with both methods were related. However, only about half of the reducing activity (fructosamine) was due to specific nonenzymatic glycation of proteins in healthy subjects and well-controlled diabetics. The remaining unspecific activity varied from serum to serum. It was not reducible with NaBH4 and was independent of the glycation of albumin, which normally accounts for about 80% of glycated serum proteins. The fructosamine assay is therefore of limited specificity for the exact measurement of glycated proteins in serum.
我们将健康受试者和糖尿病患者血清中的果糖胺活性与通过液相色谱法检测的蛋白质糖化程度进行了比较。后一种技术将ε-氨基果糖赖氨酸水解后的特定产物糠氨酸作为检测指标。我们的结果表明，果糖胺检测能够正确测量纯化的人血清白蛋白的糖化程度。另一方面，我们发现健康受试者血清的两种检测方法之间没有相关性，尽管糖尿病患者血清的两种方法检测值相关。然而，在健康受试者和血糖控制良好的糖尿病患者中，只有约一半的还原活性（果糖胺）是由蛋白质的特异性非酶糖基化引起的。其余的非特异性活性因血清而异。它不能被硼氢化钠还原，且与白蛋白糖化无关，而白蛋白糖化通常占糖化血清蛋白的80%左右。因此，果糖胺检测在精确测量血清糖化蛋白方面的特异性有限。
