Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/3365
Title: Hepatoprotective mechanism of crinum asiaticum L and lycorine in carbon tetrachloride induced oxidative stress in swiss albino mice
Researcher: Ilavenil, S
Guide(s): Ravikumar, S
Keywords: Oxidative stress
Metabolic and genetic disorders
Crinum asiaticum and lycorine MALDI-TOF
Free radicals.
Biochemistry
Biotechnology
Science
Upload Date: 18-Apr-2012
University: Prist University
Completed Date: April, 2011
Abstract: Oxidative stress is a major cause of several metabolic and genetic disorders. Natural antioxidants have an edge over synthetic ones with respect to safety concern, health benefits, potency and availability. Ever since the discovery of crude drugs from natural resources, there have been an urge to characterize and validate the bioactivity using modern techniques. The present investigation was designed to screen and validate the biopotency of the Crinum asiaticum (L) and lycorine in averting oxidative damage caused by carbon tetra chloride using Swiss albino mice as the model system. Two dimensional gel electrophoresis, MALDI-TOF and peptide mass fingerprint analyses revealed differential protein expression in the liver of the CCl4 induced, C.asiaticum and lycorine treated mice. HSP60, ATP synthase and Regucalcin have been identified, the up-regulation of which has significant role in maintaining the integrity of cellular proteins, ATP production, and calcium regulation. The hepatoprotective activity of Crinum asiaticum and lycorine was assessed from the assay of serum and liver pathological markers such as Aspartate Transaminase (AST), Alanine Transaminase (ALT), Lactate Dehydrogenase (LDH) and Alkaline Phosphatase (ALP) besides ascertaining the serum, hepatic and mitochondrial antioxidant status in control and experimental groups of mice. The contents of enzymatic and non-enzymatic antioxidants showed variations between the control and treatment groups. The extent of damage due to oxidative stress was evidenced from the banding patterns of matrix metalloproteinase and Lactate dehydrogenase.
Pagination: v, 116p.
URI: http://hdl.handle.net/10603/3365
Appears in Departments:Department Of Biotechnology

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01_title.pdfAttached File102.2 kBAdobe PDFView/Open
02_declaration.pdf94.08 kBAdobe PDFView/Open
03_certificate.pdf350.62 kBAdobe PDFView/Open
04_acknowledgements.pdf115.05 kBAdobe PDFView/Open
05_abstract.pdf84.22 kBAdobe PDFView/Open
06_graphical abstract.pdf149.25 kBAdobe PDFView/Open
07_content.pdf137.56 kBAdobe PDFView/Open
08_abbreviations.pdf111.12 kBAdobe PDFView/Open
09_list of tables.pdf129.83 kBAdobe PDFView/Open
10_list of figures.pdf201.93 kBAdobe PDFView/Open
11_chapter 1.pdf1.82 MBAdobe PDFView/Open
12_chapter 2.pdf1.31 MBAdobe PDFView/Open
13_chapter 3.pdf1.21 MBAdobe PDFView/Open
14_chapter 4.pdf337.22 kBAdobe PDFView/Open
15_chapter 5.pdf371.4 kBAdobe PDFView/Open
16_chapter 6.pdf1.35 MBAdobe PDFView/Open
17_chapter 7.pdf503.19 kBAdobe PDFView/Open
18_summary.pdf229.77 kBAdobe PDFView/Open
19_references.pdf347.44 kBAdobe PDFView/Open
20_list of publications.pdf216.42 kBAdobe PDFView/Open


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