Showing 5 results for Albumin
Afsane Talaei, Saber Jabari, Mohammad Hassan Bigdeli, Heidar Farahani,
Volume 10, Issue 4 (12-2007)
Abstract
Introduction: Diabetes is the most important metabolic disease in human. The prevalence of both types of diabetes is rapidly increasing ocross the world. Diabetes causes many complications including End Stage Renal Disease (ESRD). Diabetes is responsible for 30% of ESRD. The prevalence of diabetic nephropathy in Iran is also high. Many of these patients are becoming dialysis dependent. Many studies have shown the changes of trace metals’ levels in diabetic patients including Copper, Zinc, Manganese and Chromium. This study evaluates the correlation between urinary Copper and diabetic nephropathy Materials and Methods: This is a case-control study. Samples were selected among type 2 diabetic patients attending to diabetes clinic in Vali-e-Asr hospital in Arak. Diabetic patients were divided in two groups based on microalbuminuria, 42 patients in case and 40 patients in control group. Then the patients were classified based on duration of diabetes into 4 groups and based on the HbA1c into two groups. Then urinary Copper was determined with atomic absorption spectophotometry and compared. Independent t-test was used to analyze data. Results: Patients were 28.1% male and 69.9% female in case group and 37.5% male and 62.5% female in control group. The mean Copper level was 36.14µg /L (14.54-57.74) in case group and 14.77% µg /L (10.17-19.37) in control group. There was a statistically significant difference between the two groups (p=0.003). Conclusion: The results show a positive relation between urinary Copper and diabetic nephropathy and confirmed the results of other studies that reported the elevation of Copper in microalbuminuria. This study also showed that age, gender, duration of diabetes and HbA1c level have no effect on urinary Copper.
Fariba Faraji, Abbas S. Lotfi, Falamaki, Abdolamir Allameh, Afshin Mohsenifar, Batul Etemadikia, Ali Mota,
Volume 13, Issue 4 (1-2011)
Abstract
Background: Aflatoxins, especially aflatoxin B1, have lethal effects on human and animal health. This study is intended to present a specific, sensitive, and relatively fast method for measurement, detection, and isolation of aflatoxin-albumin (Af-Alb) adducts in serum. Materials and Methods: In this experimental-trial, three groups of rats were selected and used as positive control (treated with aflatoxin B1), negative control (without treatment) and standard (treated with radioactive aflatoxin B1). After drawing blood samples from the rats, blood serum and then, serum albumin were isolated. Albumin was hydrolyzed by pronase and eventually, was injected into HPLC system. The sample was then identified and measured by fluorescence detector. Results: Electrophoresis on PAGE revealed albumin isolated from serum to be perfectly pure. In HPLC method, detection limit for the measurement of Af-Alb adduct was determined to be 60 pg/ml. The mean of aflatoxin positive control rats serum was 19.2 ng/mg albumin. In inter- and intra-group experiments, a remarkable level of reproducibility was seen for this method. Conclusion: The amount of Af-Alb adduct is proportionate to the amount of aflatoxin received. This project was conducted with rat serum sample, but since albumin is hydrolyzed and can be isolated from aflatoxin, this method is applicable to the measurement of Af-Alb adducts in human serum samples.
Hadi Ansarihadipour, Maryamsadat Alhoseini, Soheila Rostami , Narges Farahani, Mahya Hashemi ,
Volume 15, Issue 2 (6-2012)
Abstract
Background: The aim of this study is to assess antioxidative and pro-oxidative efficacy of ascorbate on serum albumin during iron-induced oxidative stress. Materials and Methods: In this experimental study, albumin was placed in the oxidative system containing iron ions and different concentrations of ascorbate. To monitor albumin degradation, sodium dodecyl sulfate polyacrylamide gel electrophoresis was performed according to Laemmli procedure. Oxidative modification of albumin was demonstrated using a method for determination of carbonyl groups by 2,4-dinitrophenylhydrazine. Results: By applying the carbonyl assay, ascorbate showed a dual effect: initial pro-oxidative effect on albumin changed to an antioxidant one in a dose-dependent manner. Our findings showed prooxidant effects for ascorbate in low concentrations (0-100 µM) and antioxidant effects in higher concentrations (100-300 µM). Also, electrophoretic pattern of plasma proteins showed significant protein aggregations in the range of 35 to 45 kDa of MW and protein degradations in the range of 115 to 180 kDa. Conclusion: Ascorbate can produce reactive oxygen species and can also inhibit the production of these oxidants in the presence of iron ions as well. These findings may be directly applicable to oxidative states during the administration of ascorbate and may be important in preventing oxidative modifications of proteins in blood circulation and other biological fluids.
Shahrzad Hadichegeni, Bahram Goliaei, Mehrdad Hsahemi,
Volume 18, Issue 7 (10-2015)
Abstract
Background: Human serum albumin (HSA) is a soluble blood protein which can bind to small molecules (such as drugs and toxins) and transfer them within the blood circulation.
Materials and Methods: UV-Vis spectroscopy and FT-IR methods were used to characterize the binding properties of HSA with diazinon(the toxin of organophosphate) and to investigate the changes of protein secondary structure, respectively, in molecular level under physiological condition in two times of first and thirty five days .
Results: The binding constant (KDiazinon-HSA = 3.367 ) was have been calculated based UV-Vis spectroscopy data. In FT-IR method, the proportion of decrease in percentage of &alpha-Helix on the first day was 53.97% to 51.88%, other secondary structures increased, such as Turns from 8.49% to10.21%, ß-Sheet from 13.94% to 14.81%, &beta-anti from 8.2% to %8.25 and r-coils from 15.4% to % 17.24. These changes for &alpha-Helixes, Turns, ß-Sheet, &beta- anti and random r-coils after thirty five days were 56.7% to 47.11%, 25.3% to 29.75%, 6.93% to 10.94%, 2% to 2.83% and 9.08% to 10.86%, respectively.
Conclusion: Since the content of protein secondary structure relates closely with its biological activity, therefore, a decrease in &alpha-helix and increase in &beta-sheet structure in the presence of diazinon at high concentration means the decrease of HSA biological activity. Our results suggest that diazinon has a relatively good binding with HSA and it could cause considerable changes in various secondary structures and likely is indicative of a unfolding of protein especially for the samples in thirty five days .
Shahrzad Hadi Chegni1, Mohammad Taghizadeh, Bahram Goliaei,
Volume 22, Issue 6 (1-2020)
Abstract
Background and Aim: Human Serum Albumin (HSA) is one of the most abundant proteins in the blood vascular system which regulates the transportation of many chemical compounds and molecules. The purpose of this study is to review the studies about the effects of three groups of pesticides (Insecticides, herbicides and fungicides) on the molecular structure of HSA protein.
Methods & Materials: This systematic review covers 35 studies of biophysical studies of the effect of pesticides on HSA protein. These papers were searched in PubMed, Science Direct, Web of Science databases and using Google Scholar search engine among those published from 1980 to 2019.
Ethical Considerations: In this study, all ethical principles were considered.
Results: Given the close relationship between biological activities of HSA and its secondary structure, the most of the reviewed articles analyzed the secondary structures of the HSA using various biophysical methods such as Fourier Transform Infrared (FTIR), Circular Dichroism (CD) and computational analysis. In general, HSA-pesticides interactions can cause a reduction in α-helix structure and an increase in other secondary structures including β-sheet, β-anti, and random coils. In the most reports, it has been proven that the pesticides interact with HSA through hydrophobic and electrostatic interactions and hydrogen bonding. These interactions take place in the IIA subdomain (Site 1) of HSA. The binding constants of these interactions were in the range of 10 3 to 10 6 M-1.
Conclusion : The changes around the single important tryptophan residue of HSA (Trp-214) induce conformational deformity in the IIA subdomain of this protein which causes the loss of its native structure and leads to a decrease in free HSA concentrations which subsequently interrupts the transport of the essential compounds like drugs and hormones in the blood vascular system.
