Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus
A 24 kDa protein was purified from the seeds of L. sativus by ammonium sulfate fractionation and ion-exchange chromatography. Crystals were obtained by the hanging-drop vapour-diffusion method. 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 P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 43.5, b = 82.7, c = 153.4 Å.
- OSTI ID:
- 22360156
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 9; Other Information: PMCID: PMC2242876; PMID: 16946466; PUBLISHER-ID: ll5071; OAI: oai:pubmedcentral.nih.gov:2242876; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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