SPECTROSCOPIC STUDIES ON THE INTERACTION OF HUMAN SERUM ALBUMIN (HSA) WITH SURFACTIN

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

DEHGHAN NOUDEH GH.R.; HOSSEINDOKHT M.R.; FAZLI BAZAZ B.S.

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Iranian Journal of Basic Medical Sciences Year:2005 | Volume:8 | Issue:4 (28) Page(s): 289-294

Download Full-Text

View:

262

Download:

Cites:

Information Journal Paper

Title

SPECTROSCOPIC STUDIES ON THE INTERACTION OF HUMAN SERUM ALBUMIN (HSA) WITH SURFACTIN

Author(s)

DEHGHAN NOUDEH GH.R. | HOSSEINDOKHT M.R. | FAZLI BAZAZ B.S. | Issue Writer Certificate

Keywords

HUMAN SERUM ALBUMIN

SURFACTIN

STABILITY

INTERACTION

SPECTROSCOPY

Abstract

Objective: SURFACTIN, a crystalline peptide lipid surfactant produced by Bacillus subtilis, inhibits fibrin clot formation. HUMAN SERUM ALBUMIN (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport a great variety of metabolites and drugs such as anticoagulants. In the present work, the INTERACTION of HAS with SURFACTIN in solution as a function of concentration is reported.Materials and methods: The structure of HSA at different pH values in the absence and presence of SURFACTIN was investigated by fluorescence and circular dichroism (CD) spectroscopies. The different effects of surf actin upon binding to HSA are interpreted based on considerations of the expected changes in the vicinity of tryptophan residue W214.Results: The results of fluorescence and CD showed that HSA partially unfolded at pH 3.0 and 10.0 in comparison with pH 7.0. At pH 7.0 and 10.0, surf actin at low concentrations caused a red shift of maximum emission and at high concentrations a blue shift of maximum emission, which should mean unfolding after partial folding. But, compare with other pH values (pH 7.0 and 10.0), in pH 3.0, surf actin does not have considerable effect. STABILITY of HSA obtained at pH 7.0 and 10.0. ΔG (H2O) was about 15 kJmol-1 at pH 7.0 and pH 10.0.Conclusion: SURFACTIN can denature HSA at very low concentration (0.01 mM). This effect is very similar to synthetic anionic surfactants such as sodium dodecyl sulfate.

Cites

No record.

References

No record.

Cite

APA: Copy

DEHGHAN NOUDEH, GH.R., HOSSEINDOKHT, M.R., & FAZLI BAZAZ, B.S.. (2005). SPECTROSCOPIC STUDIES ON THE INTERACTION OF HUMAN SERUM ALBUMIN (HSA) WITH SURFACTIN. IRANIAN JOURNAL OF BASIC MEDICAL SCIENCES, 8(4 (28)), 289-294. SID. https://sid.ir/paper/535960/en

Vancouver: Copy

DEHGHAN NOUDEH GH.R., HOSSEINDOKHT M.R., FAZLI BAZAZ B.S.. SPECTROSCOPIC STUDIES ON THE INTERACTION OF HUMAN SERUM ALBUMIN (HSA) WITH SURFACTIN. IRANIAN JOURNAL OF BASIC MEDICAL SCIENCES[Internet]. 2005;8(4 (28)):289-294. Available from: https://sid.ir/paper/535960/en

IEEE: Copy

GH.R. DEHGHAN NOUDEH, M.R. HOSSEINDOKHT, and B.S. FAZLI BAZAZ, “SPECTROSCOPIC STUDIES ON THE INTERACTION OF HUMAN SERUM ALBUMIN (HSA) WITH SURFACTIN,” IRANIAN JOURNAL OF BASIC MEDICAL SCIENCES, vol. 8, no. 4 (28), pp. 289–294, 2005, [Online]. Available: https://sid.ir/paper/535960/en

Related Journal Papers

No record.

Related Seminar Papers

No record.

Related Plans

No record.

Recommended Workshops