Open AccessPurification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus
Author(s) -
Sethi Dhruv K.,
Qureshi Insaf A.,
Salunke Dinakar M.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106028077
Subject(s) - lathyrus , sativum , pisum , homology (biology) , albumin , ammonium sulfate , fractionation , ammonium , chemistry , biochemistry , chromatography , biology , amino acid , botany , organic chemistry
A 24 kDa protein was purified from the seeds of Lathyrus sativus by ammonium sulfate fractionation and ion‐exchange chromatography. The N‐terminal amino‐acid sequence showed significant homology with the 2S albumin class of seed storage proteins. The protein showed 85% sequence homology with the seed albumin of Pisum sativum within the 40 N‐terminal residues. Crystals were obtained by the hanging‐drop vapour‐diffusion method. The crystals belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 43.5, b = 82.7, c = 153.4 Å.