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

dc.contributor.author	Qureshi, Insaf A.
dc.contributor.author	Sethi, Dhruv K.
dc.contributor.author	Salunke, Dinakar M.
dc.date.accessioned	2022-03-27T05:19:59Z
dc.date.available	2022-03-27T05:19:59Z
dc.date.issued	2006-09-01
dc.description.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. © 2006 International Union of Crystallography All rights reserved.
dc.identifier.citation	Acta Crystallographica Section F: Structural Biology and Crystallization Communications. v.62(9)
dc.identifier.issn	17443091
dc.identifier.uri	10.1107/S1744309106028077
dc.identifier.uri	http://scripts.iucr.org/cgi-bin/paper?S1744309106028077
dc.identifier.uri	https://dspace.uohyd.ac.in/handle/1/8115
dc.title	Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus
dc.type	Journal. Article
dspace.entity.type

Now showing 1 - 1 of 1