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蛋白质的非酶糖化(non-enzymatic glycation)在糖尿病及其并发症的发生发展中起着重要作用。糖化血红蛋白(hemoglobin A1c,HbA1C)已作为糖尿病患者血糖控制的“金标准”。相对而言,同为血红素蛋白的肌红蛋白(myoglobin,Mb),其非酶糖化的研究相对较少。研究发现:非酶糖化能改变Mb的空间构象,且对Mb血红素活性中心产生一定的影响,从而导致Mb各种生物学功能发生一定程度的改变。本文综述非酶糖化对Mb结构与功能的影响的研究现状,旨在阐明Mb非酶糖化后的结构-性质-功能之间的关系及其生物学意义,为糖尿病及其并发症的发病机制研究提供新的线索。
Non-enzymatic glycation of proteins plays an important role in the development of diabetes and its complications. Glycated hemoglobin (hemoglobin A1c, HbA1C) has been used as a glycemic control in patients with “gold standard”. In contrast, the same hemoglobin myoglobin (myoglobin, Mb), its non-enzymatic glycation relatively few studies. It is found that non-enzymatic glycation can change the spatial conformation of Mb and affect the Mb heme active center to a certain extent, leading to a certain degree of change of various biological functions of Mb. This review summarizes the current research on the effect of non-enzymatic glycation on the structure and function of Mb, aiming to elucidate the relationship between the structure-property-function of non-enzymatic glycation Mb and its biological significance, and to study the pathogenesis of diabetes mellitus and its complications Provide new clues.