Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan)

被引：10

作者：

Balasubramanian, Anuradha ^{[1
]}

Ponnuraj, Karthe ^{[1
]}

机构：

[1] Univ Madras, Ctr Adv Study Crystallog & Biophys, Madras 600025, Tamil Nadu, India

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

关键词：

D O I：

10.1107/S1744309108016849

中图分类号：

Q5 [生物化学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Urease is a seed protein that is common to most Leguminosae. It also occurs in many bacteria, fungi and several species of yeast. Urease catalyzes the hydrolysis of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source. Urease from pigeon pea seeds has been purified to electrophoretic homogeneity using a series of steps involving ammonium sulfate fractionation, acid precipitation, ion-exchange and size-exclusion chromatography techniques. The pigeon pea urease was crystallized and the resulting crystals diffracted to 2.5 angstrom resolution. The crystals belong to the rhombohedral space group R32, with unit-cell parameters a = b = 176.29, c = 346.44 angstrom.

引用

页码：662 / 664

页数：3

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