MINIREVIEW ON STRUCTURAL CHANGES OF GLYCATED HUMAN SERUM ALBUMIN

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.

SATAR AHMADI N.; MOUSAVI MOVAHEDI ALI AKBAR

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

Journal Paper

Paper Information

Journal: Iranian Journal of Diabetes and Metabolism Year:2007 | Volume:7 | Issue:1 (22) Page(s): 9-22

Download Full-Text

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

Persian Verion

View:

1,187

Download:

Cites:

Information Journal Paper

Title

MINIREVIEW ON STRUCTURAL CHANGES OF GLYCATED HUMAN SERUM ALBUMIN

Author(s)

SATAR AHMADI N. | MOUSAVI MOVAHEDI ALI AKBAR | Issue Writer Certificate

Keywords

GLYCATIONQ3

SERUM ALBUMINQ2

FIBRILQ3

MOLTEN GLOBULEQ3

ALGINATEQ3

CONFORMATIONAL CHANGESQ3

Abstract

The interaction of reducing carbohydrates with proteins leads to a cascade of reactions that are known as GLYCATION or Maillard reaction that have important roles in diabetic complications. In this minireview, structural changes of glycated human SERUM ALBUMIN (GHSA) via various sugars in different incubation times, which reported in scientific literature as well as our research, were reported. Our studies showed GLYCATION induced structural changes for Human SERUM ALBUMIN (HSA). In GLYCATION process of HSA after 21 days incubation, glucose separates from HSA and induced the formation of MOLTEN GLOBULE state that is relative to several diseases that originate from MOLTEN GLOBULE state in proteins. Also, GLYCATION of HSA induced aggregation states and amyloid formation as well as decreased surface tension which plays a role of denaturant for protein as a surfactant. In following, we showed that ALGINATE as a sugar polymer decreased GLYCATION reaction in HSA. Finally, it is compared the structural changes of artificial and in vitro interaction of sugars with HSA as well as diabetic patients HSA. The results show the number of arginine residues in HSA of diabetic patients is more modified relative to lab samples.

Cites

No record.

References

No record.

Cite

APA: Copy

SATAR AHMADI, N., & MOUSAVI MOVAHEDI, ALI AKBAR. (2007). MINIREVIEW ON STRUCTURAL CHANGES OF GLYCATED HUMAN SERUM ALBUMIN. JOURNAL OF DIABETES AND METABOLIC DISORDERS, 7(1 (22)), 9-22. SID. https://sid.ir/paper/53926/en

Vancouver: Copy

SATAR AHMADI N., MOUSAVI MOVAHEDI ALI AKBAR. MINIREVIEW ON STRUCTURAL CHANGES OF GLYCATED HUMAN SERUM ALBUMIN. JOURNAL OF DIABETES AND METABOLIC DISORDERS[Internet]. 2007;7(1 (22)):9-22. Available from: https://sid.ir/paper/53926/en

IEEE: Copy

N. SATAR AHMADI, and ALI AKBAR MOUSAVI MOVAHEDI, “MINIREVIEW ON STRUCTURAL CHANGES OF GLYCATED HUMAN SERUM ALBUMIN,” JOURNAL OF DIABETES AND METABOLIC DISORDERS, vol. 7, no. 1 (22), pp. 9–22, 2007, [Online]. Available: https://sid.ir/paper/53926/en

Related Journal Papers