title: Purification, crystallization and preliminary X-ray analysis of urease from jack bean (Canavalia ensiformis).
abstract: Plant urease is a seed protein that is common in most legumes. It is also common in many bacteria and fungi and several species of yeast. Urease allows organisms to use exogenous and internally generated urea as a nitrogen source by catalyzing the hydrolysis of urea to ammonia and carbon dioxide. Urease from jack bean meal was purified to electrophoretic homogeneity using a series of steps involving acetone precipitation and size-exclusion and ion-exchange chromatography. The jack bean urease was crystallized and the resulting crystals diffracted to 2.05 A resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 138.57, c = 198.36 A.
authors.affiliation: Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, India.
authors.forename: Anuradha
authors.initials: A
authors.lastname: Balasubramanian
authors.forename: Karthe
authors.initials: K
authors.lastname: Ponnuraj
mesh_terms: D032449:Canavalia / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D014510:Urease / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D014510:Urease