Poormolaie, N. (2015) Study of thermal analysis of human serum albumin domains in diabetic and non-diabetic conditions and investigation of glucose bond using FTIR. Masters thesis, university of zabol.
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Study of thermal analysis of human serum albumin domains in diabetic and non-diabetic conditions.pdf Download (171kB) | Preview |
Abstract
Resistance of a protein against a denaturant agent is a useful property. In the current research, the domains thermal unfolding of glycated human serum albumin (GHSA) and human serum albumin (HSA) were studied under incubation at physiological conditions for 35 days. The domains thermal unfolding of GHSA and HSA were evaluated using differential scanning calorimetry (DSC), circular dichroism (CD), fourier transform infrared (FTIR) and UV–Vis spectroscopy. The results showed that the first energetic domain of GHSA remained after cooling back from 80 ºC, while the first energetic domain of HSA disappeared at this temperature. Moreover, the second energetic domain of GHSA kept on after cooling back from 90 ºC, but it disappeared in HSA at this temperate. Also, the secondary structure recovery after cooling back in GHSA was higher than HSA. Therefore, according to the obtained results, glucose can act as a stabilizer for HSA domains and can be used in food and pharmaceutical industries.
| Item Type: | Thesis (Masters) |
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| Uncontrolled Keywords: | Glycation, Proteins, Human serum albumin ,Diabetes, Thermal resistansm protein, DSC, FTIR |
| Subjects: | Q Science > QD Chemistry |
| Depositing User: | admin admin1 admin2 |
| Date Deposited: | 30 May 2017 07:38 |
| Last Modified: | 30 May 2017 07:38 |
| URI: | http://eprints.uoz.ac.ir/id/eprint/1411 |
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