Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 62(Pt 9): 869-72, 2006 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-16946466
ABSTRACT
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 P2(1)2(1)2(1), with unit-cell parameters a = 43.5, b = 82.7, c = 153.4 A.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Alérgenos
/
Lathyrus
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article