| Literature DB >> 28128054 |
Anchal Sharma1, Pramod Kumar1, Pooja Kesari1, Madhusudhanarao Katiki1, Manisha Mishra2, Pradhyumna K Singh2, Bhola R Gurjar3, Ashwani K Sharma1, Shailly Tomar1, Pravindra Kumar1.
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. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.Entities:
Keywords: 2S Albumin; IgE bindingzzm321990allergen; Wrightia tinctoria; b-cell epitope; deoxyribonucleases activity; seed storage protein
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Year: 2017 PMID: 28128054 DOI: 10.2174/0929866524666170126144936
Source DB: PubMed Journal: Protein Pept Lett ISSN: 0929-8665 Impact factor: 1.890