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Title: Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis

Abstract

The purification, identification, crystallization and preliminary crystallographic studies of an allergy-related protein, Pru du amandin, from P. dulcis nuts are reported. Food allergies appear to be one of the foremost causes of hypersensitivity reactions. Nut allergies account for most food allergies and are often permanent. The 360 kDa hexameric protein Pru du amandin, a known allergen, was purified from almonds (Prunus dulcis) by ammonium sulfate fractionation and ion-exchange chromatography. The protein was identified by a BLAST homology search against the nonredundant sequence database. Pru du amandin belongs to the 11S legumin family of seed storage proteins characterized by the presence of a cupin motif. Crystals were obtained by the hanging-drop vapour-diffusion method. The crystals belong to space group P4{sub 1} (or P4{sub 3}), with unit-cell parameters a = b = 150.7, c = 164.9 Å.

Authors:
;
Publication Date:
OSTI Identifier:
22360466
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 64; Journal Issue: Pt 1; Other Information: PMCID: PMC2373995; PMID: 18097098; PUBLISHER-ID: hc5040; OAI: oai:pubmedcentral.nih.gov:2373995; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AMMONIUM SULFATES; CRYSTALLIZATION; CRYSTALS; DIFFUSION; EXPLOSIONS; FRACTIONATION; PROTEINS; SPACE GROUPS

Citation Formats

Gaur, Vineet, Sethi, Dhruv K., and Salunke, Dinakar M., E-mail: dinakar@nii.res.in. Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis. United Kingdom: N. p., 2008. Web. doi:10.1107/S1744309107064615.
Gaur, Vineet, Sethi, Dhruv K., & Salunke, Dinakar M., E-mail: dinakar@nii.res.in. Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis. United Kingdom. https://doi.org/10.1107/S1744309107064615
Gaur, Vineet, Sethi, Dhruv K., and Salunke, Dinakar M., E-mail: dinakar@nii.res.in. 2008. "Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis". United Kingdom. https://doi.org/10.1107/S1744309107064615.
@article{osti_22360466,
title = {Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis},
author = {Gaur, Vineet and Sethi, Dhruv K. and Salunke, Dinakar M., E-mail: dinakar@nii.res.in},
abstractNote = {The purification, identification, crystallization and preliminary crystallographic studies of an allergy-related protein, Pru du amandin, from P. dulcis nuts are reported. Food allergies appear to be one of the foremost causes of hypersensitivity reactions. Nut allergies account for most food allergies and are often permanent. The 360 kDa hexameric protein Pru du amandin, a known allergen, was purified from almonds (Prunus dulcis) by ammonium sulfate fractionation and ion-exchange chromatography. The protein was identified by a BLAST homology search against the nonredundant sequence database. Pru du amandin belongs to the 11S legumin family of seed storage proteins characterized by the presence of a cupin motif. Crystals were obtained by the hanging-drop vapour-diffusion method. The crystals belong to space group P4{sub 1} (or P4{sub 3}), with unit-cell parameters a = b = 150.7, c = 164.9 Å.},
doi = {10.1107/S1744309107064615},
url = {https://www.osti.gov/biblio/22360466}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 1,
volume = 64,
place = {United Kingdom},
year = {Tue Jan 01 00:00:00 EST 2008},
month = {Tue Jan 01 00:00:00 EST 2008}
}