مطالعه کنفرماسیونی آلبومین انسانی در دماهای پایین تر از واسرشتگی با کالریمتری روبشی افتراقی، دو رنگ نمایی چرخشی و طیف سنجی (UV)یو وی

رضایی طاویرانی, مصطفی and مقدم‌نيا, سيدحسن and رنجبر, بیژن and امانی, مجتبی and مرعشی, سید امیر (1385) مطالعه کنفرماسیونی آلبومین انسانی در دماهای پایین تر از واسرشتگی با کالریمتری روبشی افتراقی، دو رنگ نمایی چرخشی و طیف سنجی (UV)یو وی. Journal of Biochemistry and Molecular Biology ــ 39 (5). pp. 530-536. شاپا 1225-8687

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Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy

English Abstract

Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from 25°C to 55°C induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. 42°C. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at 45°C and 35°C reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at 45°C compared to 35°C, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.

Item Type:Article
زبان سند : انگلیسی
نویسنده مسئول :مصطفی رضایی طاویرانی
Additional Information:cited By (since 1996) 8 Impact factor:2.207 indexing:MEDLINE / PubMed- Science citation index expended – biochemistry- biophysics index – chemical abstracts scopus - Index medicus
کلیدواژه ها (انگلیسی):dodecyl sulfate sodium; serum albumin, article; chemistry; circular dichroism; differential scanning calorimetry; human; protein binding; protein conformation; protein folding; protein secondary structure; temperature; thermodynamics; ultraviolet spectrophotometry, Calorimetry, Differential Scanning; Circular Dichroism; Humans; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Serum Albumin; Sodium Dodecyl Sulfate; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics
Subjects:QU Biochemistry
Divisions:Faculty of Medicine > Department of Basic Sciences > Department of Biophysics
ID Code:1059
Deposited By: MS Soghra Golmaghani
Deposited On:13 Dec 1388 05:10
Last Modified:20 Jan 1393 13:07

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