| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Tupe, Rashmi Kulkarni, Amruta Adeshara, Krishna Sankhe, Neena Shaikh, Shamim Dalal, Sayli Bhosale, Siddharth Gaikwad, Sushama |
| Description |
Author Affiliation: Tupe R ( Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India. Electronic address: rashmitupe@gmail.com.); Kulkarni A ( Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.); Adeshara K ( Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.); Sankhe N ( Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.); Shaikh S ( Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.); Dalal S ( Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.); Bhosale S ( Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.); Gaikwad S ( Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.) |
| Abstract |
The present work aims to investigate the concentration and time dependant effect of zinc on the in vitro non enzymatic modifications of albumin by diabetic levels of glucose. Further, preventive and curative effect of zinc was studied by adding zinc before and after initiation of glycation respectively. Glycation of albumin was done at different concentrations of zinc (125, 250 and 500 µM) at different time intervals (21, 28 and 35 days) with appropriate controls. The antiglycation potential of zinc was assessed by estimating different markers of albumin glycation (fructosamines, carbonyls, bound sugar, AGEs), structural modifications (free amino, thiol group, ß amyloid, native PAGE, ANS binding, fluorescence lifetime decay and CD analysis) and functional properties (antioxidant activity, hemolysis). Zinc at highest concentration (500 µM) significantly reduced modifications of albumin which was comparable to aminoguanidine and also protected secondary and tertiary structure of albumin after 28 days of incubation. Zinc exhibited significant protective effect on erythrocytes by inhibiting hemolysis. Thus the present study indicate preventive mode of albumin glycation inhibition by zinc. |
| File Format |
HTM / HTML |
| ISSN |
01418130 |
| Volume Number |
79 |
| e-ISSN |
18790003 |
| Journal |
International Journal of Biological Macromolecules |
| Language |
English |
| Publisher |
Elsevier |
| Publisher Date |
2015-08-01 |
| Publisher Place |
Netherlands |
| Access Restriction |
One Nation One Subscription (ONOS) |
| Subject Keyword |
Discipline Biochemistry Erythrocytes Physiology Serum Albumin, Bovine Chemistry Zinc Pharmacology Cytoprotection Drug Evaluation, Preclinical Drug Effects Glycosylation Humans Protein Processing, Post-translational Journal Article Research Support, Non-u.s. Gov't |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Structural Biology Molecular Biology Biochemistry |
