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Antioxidant, antibacterial, and cytoprotective activity of agathi leaf protein.

Zarena AS, Gopal S, Vineeth R - J Anal Methods Chem (2014)

Bottom Line: The column chromatography of the crude protein resulted in four peaks of which Peak I (P I) showed maximum inhibition activity against hydroxyl radical.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.In addition, ALP showed strong antibacterial activity against Pseudomonas aeruginosa (20 ± 3.64 mm) and Staphylococcus aureus (19 ± 1.53 mm) at 200  μ g/mL.

View Article: PubMed Central - PubMed

Affiliation: Department of Studies in Microbiology, University of Mysore, Mysore 570006, India.

ABSTRACT
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  μ M, ABTS anion (88 ± 3.22%), and DNA damage (83 ± 4.20%) at 3.44  μ 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  μ g/mL. The safety assessment showed that ALP does not induce cytotoxicity towards human lymphocyte at the tested concentration of 0.8 mg/mL.

No MeSH data available.


Related in: MedlinePlus

Inhibition of lipid peroxidation in linolenic acid micelle and erythrocyte ghost. Data are expressed as the mean ± standard deviation (n = 3). Means with different letters (a–d) are significantly different (P < 0.05).
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fig2: Inhibition of lipid peroxidation in linolenic acid micelle and erythrocyte ghost. Data are expressed as the mean ± standard deviation (n = 3). Means with different letters (a–d) are significantly different (P < 0.05).

Mentions: The in vitro peroxidation of human erythrocyte ghosts and linolenic acid micelles was used as a model system to study the free radical induced damage of biological membranes and the protective effect of ALP. Membrane lipids being rich in unsaturated fatty acids especially linoleic, linolenic, and arachidonic acids when attacked by free radicals form lipid peroxide. In the present study the antioxidant activity of the ALP was studied in comparison with known antioxidant like BHA. It was observed that the inhibitory effect of ALP in erythrocyte ghost and linolenic acid micelles was found to be 85.50 ± 6.25% and 87.67 ± 3.14% at 4.33 μM dose dependently compared to BHA which showed an activity of 84.33 ± 4.50 at 400 μM (Figure 2). Erythrocyte ghost and linolenic acid micelles are simple suitable model system commonly used in the study of LOP as the protein composition of the former is well known and they lack organelles [17]. On the other hand, linolenic acids are present in food and organisms and their oxidation results in the formation of hydroperoxides.


Antioxidant, antibacterial, and cytoprotective activity of agathi leaf protein.

Zarena AS, Gopal S, Vineeth R - J Anal Methods Chem (2014)

Inhibition of lipid peroxidation in linolenic acid micelle and erythrocyte ghost. Data are expressed as the mean ± standard deviation (n = 3). Means with different letters (a–d) are significantly different (P < 0.05).
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3927847&req=5

fig2: Inhibition of lipid peroxidation in linolenic acid micelle and erythrocyte ghost. Data are expressed as the mean ± standard deviation (n = 3). Means with different letters (a–d) are significantly different (P < 0.05).
Mentions: The in vitro peroxidation of human erythrocyte ghosts and linolenic acid micelles was used as a model system to study the free radical induced damage of biological membranes and the protective effect of ALP. Membrane lipids being rich in unsaturated fatty acids especially linoleic, linolenic, and arachidonic acids when attacked by free radicals form lipid peroxide. In the present study the antioxidant activity of the ALP was studied in comparison with known antioxidant like BHA. It was observed that the inhibitory effect of ALP in erythrocyte ghost and linolenic acid micelles was found to be 85.50 ± 6.25% and 87.67 ± 3.14% at 4.33 μM dose dependently compared to BHA which showed an activity of 84.33 ± 4.50 at 400 μM (Figure 2). Erythrocyte ghost and linolenic acid micelles are simple suitable model system commonly used in the study of LOP as the protein composition of the former is well known and they lack organelles [17]. On the other hand, linolenic acids are present in food and organisms and their oxidation results in the formation of hydroperoxides.

Bottom Line: The column chromatography of the crude protein resulted in four peaks of which Peak I (P I) showed maximum inhibition activity against hydroxyl radical.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.In addition, ALP showed strong antibacterial activity against Pseudomonas aeruginosa (20 ± 3.64 mm) and Staphylococcus aureus (19 ± 1.53 mm) at 200  μ g/mL.

View Article: PubMed Central - PubMed

Affiliation: Department of Studies in Microbiology, University of Mysore, Mysore 570006, India.

ABSTRACT
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  μ M, ABTS anion (88 ± 3.22%), and DNA damage (83 ± 4.20%) at 3.44  μ 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  μ g/mL. The safety assessment showed that ALP does not induce cytotoxicity towards human lymphocyte at the tested concentration of 0.8 mg/mL.

No MeSH data available.


Related in: MedlinePlus