Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus

Qureshi, I. A. ; Sethi, D. K. ; Salunke, D. M. (2006) Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus Acta Crystallographica Section F, 62 . pp. 869-872. ISSN 1744-3091

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Official URL: http://scripts.iucr.org/cgi-bin/paper?S17443091060...

Related URL: http://dx.doi.org/10.1107/S1744309106028077

Abstract

A 24 kDa protein was purified from the seeds of Lathyrus sativus by ammonium sulfate fractionation and ion-exchange chromatography. The N-terminal amino-acid sequence showed significant homology with the 2S albumin class of seed storage proteins. The protein showed 85% sequence homology with the seed albumin of Pisum sativum within the 40 N-terminal residues. Crystals were obtained by the hanging-drop vapour-diffusion method. The crystals belonged to space group P212121, with unit-cell parameters a = 43.5, b = 82.7, c = 153.4 Å.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Lathyrus Sativus; Allergenic Protein
ID Code:52559
Deposited On:04 Aug 2011 08:04
Last Modified:04 Aug 2011 08:04

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