Open AccessPurification, identification and preliminary crystallographic studies of a 2S albumin seed protein from Lens culinaris
Author(s) -
Gupta Pankaj,
Gaur Vineet,
Salunke Dinakar M.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108021970
Subject(s) - lens (geology) , albumin , identification (biology) , crystallography , chemistry , chromatography , biochemistry , biology , botany , paleontology
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 Å resolution and were indexed in space group P 4 1 (or P 4 3 ), with unit‐cell parameters a = b = 78.6, c = 135.2 Å.