title: Purification, identification and preliminary crystallographic studies of a 2S albumin seed protein from Lens culinaris.
abstract: Lens culinaris (lentil) is a widely consumed high-protein-content leguminous crop. A 2S albumin protein (26.5 kDa) has been identified using NH(2)-terminal sequencing from a 90% ammonium sulfate saturation fraction of total L. culinaris seed protein extract. The NH(2)-terminal sequence shows very high homology to PA2, an allergy-related protein from Pisum sativum. The 2S albumin protein was purified using a combination of size-exclusion and ion-exchange chromatography. Crystals of the 2S seed albumin obtained using the hanging-drop vapour-diffusion method diffracted to 2.5 A resolution and were indexed in space group P4(1) (or P4(3)), with unit-cell parameters a = b = 78.6, c = 135.2 A.
authors.affiliation: National Institute of Immunology, New Delhi 110067, India.
authors.forename: Pankaj
authors.initials: P
authors.lastname: Gupta
authors.forename: Vineet
authors.initials: V
authors.lastname: Gaur
authors.forename: Dinakar M
authors.initials: DM
authors.lastname: Salunke
mesh_terms: D000418:Albumins / Q000737:chemistry* / Q000302:isolation & purification; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D027806:Lens Plant / Q000737:chemistry* / Q000196:embryology; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012639:Seeds / Q000737:chemistry*
chemical_list: D000418:Albumins; D010940:Plant Proteins