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Evaluating Human Serum Albumin Structure and Stability in the Presence of DTAB
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P Vasoghi *   1, N Ahmadi , M Shahani , E Bahadori monfared , M Azizi |
| 1- , padinavm@gmail.com |
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Abstract: (10078 Views) |
| Introduction: Human serum albumin with its singular structure acts as a carrier mo-lecule that can attach to a variety of sub-stances. Any structural or functional chan-ges in albumin are accompanied with unde-sirable outcomes. In the present research, attachment of some ligands such as det-ergents (DTAB) and sugars (glucose) to albumin were evaluated at temperatures 27°C and 42°C.
Materials & Methods: Tris-buffer solusion for albumin with a pH close to the pH of body was prepared. To denature albumin, hydrochloric acid was used. UV spectero-photometric technique was applied to eval-uate denaturation process.
Findings: With increment of DTAB conc-entration the maximum optical absorption of albumin decreased. Glucose concent-ration at 400mg/dl level caused a profound change in the optical absorption of albumin that might affect the structure of the mo-lecule.
Discussion & Conclusion: Glucose elevate-on has deleterious effects and deteriorates the function of many molecules in blood. The effects may exert on hormones, drug transportation, necessary ions and elements |
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| Keywords: Human serum albumin, DTAB cation, glucose, thermal denaturation, UV spectrophotometry |
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Full-Text [PDF 447 kb]
(3793 Downloads)
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Type of Study: Research |
Subject:
anatomy
Received: 2014/02/18 | Accepted: 2014/02/18 | Published: 2014/02/18
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