Gupta, Pankaj ; Gaur, Vineet ; Salunke, Dinakar M. (2008) Purification, identification and preliminary crystallographic studies of a 2S albumin seed protein from Lens culinaris Acta Crystallographica Section F, 64 (8). pp. 733-736. ISSN 1744-3091
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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S174430...
Related URL: http://dx.doi.org/10.1107/S1744309108021970
Abstract
Lens culinaris (lentil) is a widely consumed high-protein-content leguminous crop. A 2S albumin protein (26.5 kDa) has been identified using NH2-terminal sequencing from a 90% ammonium sulfate saturation fraction of total L. culinaris seed protein extract. The NH2-terminal sequence shows very high homology to PA2, an allergy-related protein from Pisum sativum. The 2S albumin protein was purified using a combination of size-exclusion and ion-exchange chromatography. Crystals of the 2S seed albumin obtained using the hanging-drop vapour-diffusion method diffracted to 2.5 Å resolution and were indexed in space group P41 (or P43), with unit-cell parameters a = b = 78.6, c = 135.2 Å.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to John Wiley and Sons. |
| Keywords: | Allergies; Food Allergens; 2S Seed Albumins; Nh2-terminal Sequencing |
| ID Code: | 52624 |
| Deposited On: | 04 Aug 2011 08:06 |
| Last Modified: | 04 Aug 2011 08:06 |
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