full issue - Association of Biotechnology and Pharmacy
full issue - Association of Biotechnology and Pharmacy
full issue - Association of Biotechnology and Pharmacy
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Current Trends in <strong>Biotechnology</strong> <strong>and</strong> <strong>Pharmacy</strong>Vol. 5 (1) 1073-1082 January 2011. ISSN 0973-8916 (Print), 2230-7303 (Online)1079peroxidase <strong>and</strong> glutathionetransferase, is readilyavailable to neutralize the free radicals generatedby t-BHP.SOD catalyses the depletion <strong>of</strong> thesuperoxide radical <strong>and</strong> protects oxygenmetabolizingcells against harmful effects <strong>of</strong>superoxide free radicals. Some types <strong>of</strong> SODlike MnSOD which contains a manganeseprosthetic group, resides in the mitochondria,perhaps because <strong>of</strong> the need to protectmitochondrial proteins, membranes, <strong>and</strong> DNAfrom . O 2generated as a result <strong>of</strong> the respiratorychain. Figure 5 showing total SOD levels in humanerythrocytes with reference to sub fraction F2-3.SOD levels in 12.5 µg/ml treated group at thetime intervals <strong>of</strong> 0, 30, 60, 90 min, t-BHP-control<strong>and</strong> control were 1.2, 1.9, 3, 3.23, 1.85 <strong>and</strong> 11.02IU/g Hb protein at the concentration <strong>of</strong> 25 µg/mlMDA, SOD levels were 1.22, 2.5, 5.2 <strong>and</strong> 5.2<strong>and</strong> at the concentration <strong>of</strong> 50 µg/ml SOD levelswere 1.1, 5.3, 9.4 <strong>and</strong> 9.7 IU/g Hb, respectively(Fig.5).CAT, a soluble protein in erythrocytes, playsa role in the decomposition <strong>of</strong> hydrogen peroxideto give H 2O. In humans, the highest levels <strong>of</strong>Fig. 5. Effect <strong>of</strong> fraction F2-3 on t-BHP induced oxidativestress in erythrocytes was monitored by measuringthe superoxide dismutase activity. Results are mean ±SD.catalase are found in liver, kidney <strong>and</strong> erythrocytes,where it is believed to account for the majority <strong>of</strong>hydrogen peroxide decomposition. Figure 6showing catalase activity in human erythrocyteswith reference to FME sub fraction F2-3. CATlevels in 12.5 µg/ml treated group at the timeintervals <strong>of</strong> 0, 30, 60, 90 min, t-BHP-control <strong>and</strong>control were 50.1, 55.4, 61.8, 62.4, 53.9 <strong>and</strong> 99.78µmol H 2O 2/g Hb/min. at the concentration <strong>of</strong> 25µg/ml MDA levels were 52.8, 60.9, 72.3 <strong>and</strong> 76.6<strong>and</strong> at the concentration <strong>of</strong> 50 µg/ml MDA levelswere 51.1, 62.5, 98.3 <strong>and</strong> 100.7 µmol H 2O 2/g Hb/min., respectively (Fig.6). Since both the enzymesSOD <strong>and</strong> CAT are directly involved in theneutralization <strong>of</strong> free radicals, these enzymes playa pivotal role in the oxidative stress. Theseenzyme levels were significantly reduced in t-BHPtreated groups indicating that antioxidant ability<strong>of</strong> the erythrocytes are reduced in t-BHP treatedgroup. Since these enzymes are replenished inresponse to F2-3 fraction <strong>of</strong> the fruit, erythrocytesagain gained the antioxidant potentials to combatagainst the free radicals generated in the variousmetabolic reactions.The present findings show that L.acutangula fruit aqueous fraction F2-3pretreatment attenuated t-BHP induced lipidperoxidation in human erythrocyes. Specifically,fraction F2-3 prevented t-BHP induced increasesin MDA levels, <strong>and</strong> concomitantly restored GSHcontent, SOD <strong>and</strong> CAT activity in erythrocytes,though to a different degrees. These effects mayreflect the ability <strong>of</strong> fraction F2-3 to enhance thescavenging <strong>and</strong> inactivation <strong>of</strong> H 2O 2<strong>and</strong> hydroxylradicals. In addition, fraction F2-3 may serve asa chealator <strong>and</strong> directly bind to Fe 2+ , whichcatalyzes formation <strong>of</strong> free radicals via the Fentonreactions (28, 29). Fraction F2-3 may alsoterminate lipid peroxidation by induction <strong>of</strong>enzymatic <strong>and</strong> non-enzymatic antioxidants, suchas GSH, SOD <strong>and</strong> CAT (30). Accordingly, theRole <strong>of</strong> Luffa acutangula in Oxidative damage