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Analysis of protein posttranslational modifications by mass spectrometry: With special reference to haemoglobin |
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| Authors: | Murali Woodi Amit Kumar Mondal Balaram Padmanabhan Krishnaswamy Patnam Rajagopalan |
| Institution: | (1) Cauvery Medical Center, Bangalore, Karnataka, India;(2) Indian Institute of Science, Bangalore, Karnataka, India;(3) St John’s Research Institute, Bangalore, Karnataka, India;(4) Cauvery Medical Center, # 43/2, Bellary road, N.H.7, Sahakara nagar, Banglore, 560 092, India |
| Abstract: | 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. |
| Keywords: | Glutathionylation Glycation Oxidative stress End-stage renal disease Renal replacement therapy |
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