Antioxidant,antibacterial,and cytoprotective activity of agathi leaf protein

In the present study a protein termed agathi leaf protein (alp) from sesbania grandiflora linn. (agathi) leaves was isolated after successive precipitation with 65% ammonium sulphate followed by purification on sephadex g 75. the column chromatography of the crude protein resulted in four peaks of which peak i (p i) showed maximum inhibition activity against hydroxyl radical. sds-page analysis of p i indicated that the molecular weight of the protein is ≈29 kda. the purity of the protein was 98.4% as determined by rp-hplc and showed a single peak with a retention time of 19.9 min. alp was able to reduce oxidative damage by scavenging lipid peroxidation against erythrocyte ghost (85.50 ± 6.25%),linolenic acid (87.67 ± 3.14%) at 4.33 m,abts anion (88 ± 3.22%),and dna damage (83 ± 4.20%) at 3.44 m in a dose-dependent manner. the purified protein offered significant protection to lymphocyte (72% at 30 min) induced damage by t-booh. in addition,alp showed strong antibacterial activity against pseudomonas aeruginosa (20 ± 3.64 mm) and staphylococcus aureus (19 ± 1.53 mm) at 200 g/ml. the safety assessment showed that alp does not induce cytotoxicity towards human lymphocyte at the tested concentration of 0.8 mg/ml. © 2014 a. s. zarena et al.