Purification, identification and preliminary crystallographic studies of a 2S albumin seed protein from Lens culinaris

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):733-6. doi: 10.1107/S1744309108021970. Epub 2008 Jul 26.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Albumins / chemistry*
  • Albumins / isolation & purification
  • Chromatography, Gel
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Lens Plant / chemistry*
  • Lens Plant / embryology
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Protein Conformation
  • Seeds / chemistry*

Substances

  • Albumins
  • Plant Proteins