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Methods Enzymol. 1997;276:307-26. doi: 10.1016/S0076-6879(97)76066-X.
2
Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis.巴旦木(扁桃)中的一种变应原蛋白——苦杏仁球蛋白的纯化、鉴定及初步晶体学研究
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):32-5. doi: 10.1107/S1744309107064615. Epub 2007 Dec 20.
3
Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus.来自草香豌豆的一种变应原蛋白的纯化、鉴定及初步晶体学研究
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt 9):869-72. doi: 10.1107/S1744309106028077. Epub 2006 Aug 11.
4
Crystallization and preliminary structure determination of the plant food allergen Pru av 2.植物食物过敏原Pru av 2的结晶及初步结构测定
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):186-8. doi: 10.1107/S1744309104033822. Epub 2005 Jan 8.
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Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.2S白蛋白型花生过敏原的结构与稳定性:对花生过敏反应严重程度的影响
Biochem J. 2006 May 1;395(3):463-72. doi: 10.1042/BJ20051728.
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Prevalence of food allergy: an overview.食物过敏的患病率:概述
Proc Nutr Soc. 2005 Nov;64(4):413-7. doi: 10.1079/pns2005458.
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Complete assignment and secondary structure of the Brazil nut allergen Ber e 1.巴西坚果过敏原Ber e 1的完整一级结构和二级结构。
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8
Gastrointestinal food allergy: new insights into pathophysiology and clinical perspectives.胃肠道食物过敏:病理生理学与临床前景的新见解
Gastroenterology. 2005 Apr;128(4):1089-113. doi: 10.1053/j.gastro.2004.08.015.
9
Molecular properties of food allergens.食物过敏原的分子特性
J Allergy Clin Immunol. 2005 Jan;115(1):14-23; quiz 24. doi: 10.1016/j.jaci.2004.10.022.
10
Purification, identification and preliminary crystallographic characterization of a novel seed protein from Vigna unguiculata.来自豇豆的一种新型种子蛋白的纯化、鉴定及初步晶体学表征
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小扁豆2S白蛋白种子蛋白的纯化、鉴定及初步晶体学研究

Purification, identification and preliminary crystallographic studies of a 2S albumin seed protein from Lens culinaris.

作者信息

Gupta Pankaj, Gaur Vineet, Salunke Dinakar M

机构信息

National Institute of Immunology, New Delhi 110067, India.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):733-6. doi: 10.1107/S1744309108021970. Epub 2008 Jul 26.

DOI:10.1107/S1744309108021970
PMID:18678944
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2494977/
Abstract

Lens culinaris (lentil) is a widely consumed high-protein-content leguminous crop. A 2S albumin protein (26.5 kDa) has been identified using NH(2)-terminal sequencing from a 90% ammonium sulfate saturation fraction of total L. culinaris seed protein extract. The NH(2)-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 A resolution and were indexed in space group P4(1) (or P4(3)), with unit-cell parameters a = b = 78.6, c = 135.2 A.

摘要

兵豆是一种被广泛食用的、高蛋白含量的豆科作物。通过对兵豆种子总蛋白提取物90%硫酸铵饱和度级分进行N端测序,已鉴定出一种2S清蛋白(26.5 kDa)。该N端序列与来自豌豆的一种过敏相关蛋白PA2具有很高的同源性。采用尺寸排阻色谱和离子交换色谱相结合的方法对2S清蛋白进行了纯化。利用悬滴气相扩散法获得的2S种子清蛋白晶体衍射分辨率为2.5 Å,并确定其空间群为P4(1)(或P4(3)),晶胞参数a = b = 78.6,c = 135.2 Å。