Résumé
Human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. Due to its long life period and high concentration in plasma, HSA is highly sensitive to glycation. It is reported that 175 mg/dL glucose concentration is a threshold of kidney activity for the beginning of excretion of glucose. PH denaturation of HSA in absence and presence of different concentrations of glucose is studied and based on the Pace two-state model, the findings are analyzed. In addition, florescence emission data of albumin range in the period of 300-500 nm was depicted. The amounts of free energy change and [D] [1/2] parameters of unfolding in correspond to florescence date indicate that glucose induces fine structural change in human serum albumin. Results showed that 175 mg/dL glucose concentration is a critical point for albumin structural and functional alteration
Résumé
Aldolase C as a glycolytic enzyme is associated with cellular structure at developmental stages of all cells, and this is particularly evident during the early stages of morphogenesis. It seems that expression of aldolase C can be regulated by the rate of differentiation that depends on the level of transcription or mRNA stability. There are several techniques to detect gene expression here proteomics was used for determining expression of aldolase C [as a differentiation factor] in several cell types and basal cell carcinoma [BCC] tissue. The human astrocytes were differentiated from mesenchymal stem cells, fibroblast cells were cultured as primary cell culture and BCC tissue was taken from the patient. The fibroblast cells divided into two groups including sham and exposed groups. The exposed cells are them that were exposed to continue Extremely Low-Frequency Electromagnetic Fields [ELF-EMF]. The analysis of 2DE gels, showed different expression of aldolase C in mentioned cells. The findings indicate that the amount of aldolase C expression decreases as differentiation process develops