PROTEIN PROFILING OF DIFFERENT PLANT TISSUES FROM HERB PHYLLANTHUS NIRURI
DOI:
https://doi.org/10.11113/jt.v77.6714Keywords:
Phyllanthus niruri, bioactive peptides, proteomicsAbstract
Herb Phyllanthus niruri (P. niruri) is known to have various pharmacological functions including anticancer, antibacterial, antioxidant, anti-hypertensive and also anti-diabetic properties. In this research, the proteomic part of P. niruri was studied to determine the bioactive peptides that responsible for specific characteristics. Total soluble proteins from different plant parts of freshly collected P. niruri were extracted using TCA/acetone method and then quantified using Bradford assay. Fruits part was found to have a significantly higher amount of proteins (4.91µg/µl + 0.21) compared to leaves (4.18µg/µl + 0.15). To determine the quality of proteins in the crude extract, SDS-Page was carried out which separates proteins in the basis of molecular weight. Proteins extracted from leaves were widely distributed between the range of 3.5 kDa to 160 kDA. Meanwhile, proteins in fruits mainly distributed within the range of 15 kDa to 80 kDa. The most highly expressed protein band was found in fruit, located in between 30 to 40 kDa. The protein extracts were then further analyzed based on the molecular weight and isoelectric points using two-dimensional gel electrophoresis (2D-GE) approach. Based on the profile pattern obtained from 2D-GE analysis, protein extract from fruits seems to express more protein spots compared to protein extract from leaves. Protein spots from fruit are seen to be intensely resolved within pH 4 to 10 at molecular weight between 10 kDa to 80 kDa. On the other hand, protein spots from leaves were moderately resolved at pH 4 to 10 at molecular weight within 10 kDa to 50 kDa.
References
America, S. 1985. Review of Literature. 4–16
Bhattacharjee, R., and Sil, P. C. 2007. Protein Isolate from the Herb Phyllanthus niruri Modulates Carbon Tetrachloride-Induced Cytotoxicity in Hepatocytes. Toxicology Mechanisms and Methods. 17: 41-47.
Bradford, M. M. 1976. A Rapid and Sensitive Method for tThe Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding. Analytical Biochemistry. 72: 248-254.
Carmo-Silva, A. E., BArta, C., and Salvucci, M. E. 2011. Isolation of Ribulose-1, 5-biphosphate carboxylase/oxygenese from Leaves. Photosynthesis Research Protocols. Springer. 339-349.
Chen, T., Qi, J. M., Xu, J. T., Chen, P. P., Tao, A. F., Chen, F. C., and Chen, W. 2011. Optimization of Two-Dimensional Gel Electrophoresis for Kenaf Leaf Proteins. Agricultural Sciences in China. 10(12): 1842-1850.
Farrell, P. H. O. 2010. NIH Public Access. 250(10): 4007-4021.
Feller, U., Anders, I., and Mae, T. 2008. Rubiscolytics: Fate of Rubisco After Its Enzymatic Function in a Cell Is Terminated. Journal of Experimental Botany. 59(7): 1615-1624.
Harish, R., and Shivanandappa, T. 2006. Antioxidant Activity and Hepatoprotective Potential of Phyllanthus niruri. Food Chemistry. 95: 180-185.
Laemmli, U. K. 1970. Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T4. Nature, 227: 680-685.
Liu, Y., Ahn, J.-E., Datta, S., Salzman, R. a, Moon, J., Huyghues-Despointes, B., … Zhu-Salzman, K. 2005. Arabidopsis Vegetative Storage Protein is an Anti-Insect Acid Phosphatase. Plant Physiology. 139(3): 1545-1556.
O’Farrell, P. H. 1975. High resolution Two-Dimensional Electrophoresis Of Proteins. The Journal of Biological Chemistry. 250(10): 4007-4021.
Ribonucleoproteins in Gene Regulation and Disease retrieved on June 28, 2015 from http://www.hhmi.org/research/ribonucleoproteins-gene-regulation-and-disease.
Sarkar, M. K., Kinter, M., Mazumder, B., and Sil, P. C. 2009. Purification and Characterisation of a Novel Antioxidant Protein Molecule from Phyllanthus niruri. Food Chemistry. 114(4): 1405-1412.
Shabeer, J., Srivastava, R. S., and Singh, S. K. 2009. Antidiabetic and Antioxidant Effect of Various Fractions of Phyllanthus Simplex in Alloxan Diabetic Rats. Journal of Ethnopharmacology. 124(1): 34-38.
Sheoran, I. S., Ross, A. R. S., Olson, D. J. H., and Sawhney, V. K. 2009. Compatibility of Plant Protein Extraction Methods with Mass Spectrometry for Proteome Analysis. Plant Science. 176: 99-104.
Sheoran, I. S., Sproule, K. a., Olson, D. J. H., Ross, a. R. S., and Sawhney, V. K. 2006. Proteome Profile and Functional Classification of Proteins in Arabidopsis Thaliana (Landsberg Erecta) Mature Pollen. Sexual Plant Reproduction. 19: 185-196. http://doi.org/10.1007/s00497-006-0035-3.
Stotz, M. M. 2012. Structure of Green Type Rubisco Activase from Nicotiana tabacum.
SWISS-2DPAGE Viewer: Arabidopsis thaliana (Mouse-ear cress) retrieved on June 28, 2015 from http://world-2dpage.expasy.org/swiss-2dpage/viewer.
Downloads
Published
Issue
Section
License
Copyright of articles that appear in Jurnal Teknologi belongs exclusively to Penerbit Universiti Teknologi Malaysia (Penerbit UTM Press). This copyright covers the rights to reproduce the article, including reprints, electronic reproductions, or any other reproductions of similar nature.
