Open AccessPurification, crystallization and preliminary X‐ray analysis of urease from pigeon pea ( Cajanus cajan )
Author(s) -
Balasubramanian Anuradha,
Ponnuraj Karthe
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108016849
Subject(s) - cajanus , urease , urea , ammonium , fractionation , hydrolysis , chemistry , crystallization , ammonium sulfate , ammonia , chromatography , biochemistry , biology , organic chemistry , agronomy
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 Å resolution. The crystals belong to the rhombohedral space group R 32, with unit‐cell parameters a = b = 176.29, c = 346.44 Å.