Woodi Murali, Mondal Amit Kumar, Padmanabhan Balaram, Rajagopalan Krishnaswamy Patnam
Cauvery Medical Center, Bangalore, Karnataka India ; Cauvery Medical Center, # 43/2, Bellary road, N.H.7, Sahakara nagar, Banglore, 560 092 India.
Indian J Clin Biochem. 2009 Jan;24(1):23-9. doi: 10.1007/s12291-009-0004-3. Epub 2009 May 8.
Mass spectrometry provides a convenient platform for the study of different protein post translational modifications from clinical specimen. Analysis of different post translational modifications of hemoglobin like glycation and glutathionylation can provide useful information on the disease progression and the possible outcome of therapies. In the present study, we have addressed post translational modifications of hemoglobin like glutathionylation and glycation in relation to diabetes and chronic renal failure. We found that both alpha and beta chains of human hemoglobin are glycated irrespective of the extent of glycemia as evidenced by a mass increment of 162 Da. The phenomenon of glutathionylation was observed with only the beta globin chain of hemoglobin probably due to the presence of an accessible cysteine residue indicated by a mass increment of 305 Da. Also, the extent of gltuathionylation observed in the CRF patients could correlate with the severity of the oxidative stress owing to renal replacement therapies like dialysis and transplantation.
质谱分析法为研究临床样本中不同的蛋白质翻译后修饰提供了一个便捷的平台。对血红蛋白不同的翻译后修饰（如糖基化和谷胱甘肽化）进行分析，可以为疾病进展和治疗的可能结果提供有用信息。在本研究中，我们探讨了与糖尿病和慢性肾衰竭相关的血红蛋白的翻译后修饰，如谷胱甘肽化和糖基化。我们发现，无论血糖水平如何，人类血红蛋白的α链和β链都会发生糖基化，质量增加162 Da即可证明这一点。仅在血红蛋白的β珠蛋白链中观察到谷胱甘肽化现象，这可能是由于存在一个可接近的半胱氨酸残基，质量增加305 Da表明了这一点。此外，在慢性肾衰竭患者中观察到的谷胱甘肽化程度可能与透析和移植等肾脏替代疗法引起的氧化应激严重程度相关。
