alexa Purification and characterization of approximately 35 kDa antioxidant protein from curry leaves (Murraya koenigii L.).


Medicinal chemistry

Author(s): Ningappa MB, Srinivas L

Abstract Share this page

Abstract Curry leaves (Murraya koenigii L. Spreng, Rutaceae) is an herbal species used in traditional medicine in eastern Asia. In this study, the antioxidant protein was purified by homogenization of curry leaves powder in Tris buffer, 65\% ammonium sulphate precipitation and gel filtration on Sephadex G-75 column which resulted in three peaks (PI, PII and PIII). PII protein inhibited lipid peroxidation in human RBC ghost at 100 microg by 80\%, whereas PI and PIII at 600 microg showed moderate antioxidant activity (40-50\%). Homogeneity of PII was confirmed by rechromatographing on Sephadex G-75 and reverse phase HPLC. The antioxidant protein (PII) from curry leaves (APC) showed apparent molecular weight of 35 kDa by SDS-PAGE and MALDI/MS analysis. The protein nature of APC was established by the presence of amino acids and loss of antioxidant activity on heat and protease treatment. The APC at 0.8 microM inhibited lipoxygenase activity by 71\%, effectively prevented diene, triene and tetraene lipids formation at 3 microM, and scavenged about 85\% hydroxyl and DPPH radicals at 150-fold lesser concentration compared to BHA and alpha-tocopherol (400 microM). In addition, APC reduced cytochrome c and ferric ion, chelated ferrous ion, and inhibited ferrous sulfate: ascorbate-induced fragmentation and sugar oxidation to 80-90\%. Thus, the present study demonstrates the in vitro characterization of antioxidant protein from the curry leaves (M. koenigii L.). This article was published in Toxicol In Vitro and referenced in Medicinal chemistry

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version