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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, identification and preliminary crystallographic characterization of a novel seed protein from Vigna unguiculata.
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Purification, identification and preliminary crystallographic characterization of a novel seed protein from Vigna unguiculata.

机译：净化、识别和初步的晶体特性的新型种子蛋白质从豇豆属unguiculata。

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摘要

A tropical legume, Vigna unguiculata, was explored in order to identify potential allergens among the abundant seed proteins and to attempt their crystallographic study. Salt fractionation of the seed extract followed by chromatographic separation led to the purification of a 25 kDa protein. Gel-filtration chromatography of the 80% ammonium sulfate precipitation fraction led to separation of this protein in pure form, which was subjected to N-terminal sequencing. The N-terminal sequences of internal fragments of this protein showed 85% homology to mung bean seed albumin. This family of proteins is known to be intrinsically allergenic. Rhombic shaped crystals were obtained that diffracted to about 2.1 A resolution. The crystals belong to space group C2 and have unit-cell parameters a = 124.9, b = 60.1, c = 67.5 A, beta = 111.1 degrees .
机译：热带豆科,豇豆属unguiculata探索以识别潜在的过敏原之一丰富的蛋白质和尝试他们的种子晶体研究。种子提取物色谱紧随其后分离导致25 kDa的净化蛋白质。硫酸铵沉淀分数了在纯粹的形式,这种蛋白质的分离受到n端序列。氨基端序列内部的碎片这种蛋白质显示,85%同源绿豆种子白蛋白。本质上是过敏。得到了晶体衍射有关2.1一项决议。集团C2,晶胞参数= 124.9,b = 60.1, c = 67.5,β= 111.1度。

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