Schleicher E, Wieland O H
Klinisch-chemisches Institut, Krankenhaus München-Schwabing, München, F.R.G.
J Clin Chem Clin Biochem. 1989 Sep;27(9):577-87.
This review of protein glycation deals with the biochemical background of glycated blood proteins, their methods of determination and their clinical significance. General reaction principles for determination of glycated proteins are discussed with special emphasis on the determination of glycated serum proteins in the clinical laboratory. Binding methods like boronate affinity, immunoassay, phenylhydrazine binding and ion exchange chromatography leave the analyte intact, whereas chemical methods like strong or mild hydrolysis or reduction in alkaline medium (fructosamine assay) results in destruction of the glycated protein. As most reactions are nonstoichiometric (except ion exchange chromatography and periodate oxidation), varying results are obtained from laboratory to laboratory. Up to now boronate affinity chromatography, mild hydrolysis yielding hydroxymethylfurfural and the fructosamine assay have been mostly used for determination of glycated serum proteins. The fructosamine assay appears to be most practical, because it is quick, economic and precise, but it suffers from unspecific side reactions. Although other methods like immunoassays or boronate ester formation in solution appear promising, there is currently no commercially available assay for the economic, precise and accurate determination of glycated serum protein. The clinical relevance of glycated serum protein determination is difficult to evaluate because the assays are based on different reaction principles and hence yield variable results. Nevertheless, the following conclusion may be drawn from the reports now available. i) The possibility that glycated serum proteins may discriminate better than glycated haemoglobin between "normal" and "diabetic" is still controversial. ii) Glycated serum proteins are formed faster than glycated haemoglobin, reflecting the changes in glycaemia for shorter periods of time (medium-term control). iii) It has not been yet established, using large cohorts, whether the glycated serum proteins allow the detection or exclusion of diabetes. iv) Determination of glycated serum proteins should not be considered as a substitute for the determination of glycated haemoglobin, but rather as a complementary determination, leading to the improved laboratory control of the diabetic patient.
本蛋白质糖化综述涉及糖化血液蛋白的生化背景、其测定方法及其临床意义。讨论了糖化蛋白测定的一般反应原理，特别强调了临床实验室中糖化血清蛋白的测定。硼酸盐亲和、免疫测定、苯肼结合和离子交换色谱等结合方法可使分析物保持完整，而强碱或弱酸水解或碱性介质还原（果糖胺测定）等化学方法会导致糖化蛋白的破坏。由于大多数反应是非化学计量的（离子交换色谱和高碘酸盐氧化除外），不同实验室获得的结果各不相同。到目前为止，硼酸盐亲和色谱、温和水解生成羟甲基糠醛和果糖胺测定法大多用于测定糖化血清蛋白。果糖胺测定法似乎最实用，因为它快速、经济且精确，但它存在非特异性副反应。尽管免疫测定或溶液中硼酸盐酯形成等其他方法看起来很有前景，但目前尚无用于经济、精确和准确测定糖化血清蛋白的商业可用测定法。糖化血清蛋白测定的临床相关性难以评估，因为这些测定基于不同的反应原理，因此产生的结果各不相同。然而，从现有报告中可以得出以下结论。i）糖化血清蛋白在区分“正常”和“糖尿病”方面可能比糖化血红蛋白表现更好的可能性仍存在争议。ii）糖化血清蛋白的形成速度比糖化血红蛋白快，反映了较短时间段内血糖的变化（中期控制）。iii）尚未通过大量队列研究确定糖化血清蛋白是否能够检测或排除糖尿病。iv）糖化血清蛋白的测定不应被视为糖化血红蛋白测定的替代方法，而应被视为一种补充测定方法，从而改善对糖尿病患者的实验室控制。
