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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, characterization and preliminary crystallographic studies of a cysteine protease from Pachyrrhizus erosus seeds.
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Purification, characterization and preliminary crystallographic studies of a cysteine protease from Pachyrrhizus erosus seeds.

机译：纯化、表征和初步的半胱氨酸蛋白酶晶体研究从Pachyrrhizus erosus种子。

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摘要

The proteins Spe31 and Spe32, named after their respective molecular weights of about 31 and 32 kDa, were purified simultaneously from the seeds of Pachyrrhizus erosus. They cannot be separated from each other by column chromatography. N-terminal sequence analysis indicated that they belonged to the papain family of cysteine proteases. An in-gel activity assay revealed that Spe31 possesses proteolytic activity while Spe32 only displays very weak activity for protein degradation. Both of them are glycoproteins as detected by the periodic acid and Schiff's reagent method. Crystals were obtained from the protein mixture by the hanging-drop vapour-diffusion method; they diffracted to a resolution of 2.61 A on an in-house X-ray source. The crystals belong to space group P4(1(3))2(1)2, with unit-cell parameters a = b = 61.96, c = 145.61 A. Gel electrophoresis under non-denaturing conditions showed that the protein crystallized was Spe31.
机译：蛋白质Spe31 Spe32,以他们的名字命名各自分子量约为31和32从种子kDa,同时净化的Pachyrrhizus erosus。通过柱色谱法从对方。氨基端序列分析表明他们属于半胱氨酸的木瓜蛋白酶家族蛋白酶。Spe31 Spe32时具有蛋白水解活性只显示非常弱的活动的蛋白质退化。被高碘酸希夫氏试剂的方法。蛋白质悬滴混合物vapour-diffusion方法;2.61解决内部的x射线源。水晶属于空间群P4 (1 (3)) 2 (1) 2,晶胞参数a = b = 61.96, c =145.61。non-denaturing条件表明,蛋白质结晶是Spe31。

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