Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus.
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.
Qureshi
Insaf A
IA
National Institute of Immunology, New Delhi 110067, India.
Sethi
Dhruv K
DK
Salunke
Dinakar M
DM
D000485:Allergens / Q000737:chemistry* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D027807:Lathyrus / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012639:Seeds
D000485:Allergens; D010940:Plant Proteins