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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.

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。

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