Purification and Characterization of 2S Albumin from Seeds of Wrightia tinctoria Exhibiting Antibacterial and DNase Activity

Author(s): Anchal Sharma, Pramod Kumar, Pooja Kesari, Neetu, Madhusudhanarao Katiki, Manisha Mishra, Pradhyumna K. Singh, Bhola R. Gurjar, Ashwani K. Sharma, Shailly Tomar, Pravindra Kumar.

Journal Name: Protein & Peptide Letters

Volume 24 , Issue 4 , 2017

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Graphical Abstract:


2S albumin is a low-molecular-weight seed storage protein belonging to the prolamin superfamily. In the present work a small 2S albumin (WTA) protein of ~16 kDa has been purified from the seeds of Wrightia tinctoria. The WTA is a heterodimer protein with a small subunit of ~5 kDa and a larger subunit of ~11 kDa bridged together through disulphide bonds. The protein exhibits deoxyribonucleases activity against closed circular pBR322 plasmid DNA and linear BL21 genomic DNA. The protein also showed antibacterial activity against Morexalla catarrhalis. CD studies indicate a high α-helical content in the protein. The conserved disulphide bonds in the protein suggest that the WTA is highly stable under high pH and temperature like other 2S albumin.

Keywords: 2S Albumin, seed storage protein, Wrightia tinctoria, deoxyribonucleases activity, b-cell epitope, IgE binding allergen.

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Article Details

Year: 2017
Page: [368 - 378]
Pages: 11
DOI: 10.2174/0929866524666170126144936
Price: $58

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