Isolation of lectin and albumin from Pisum sativum var. macrocarpon ser. cv. sugar snap

Int J Biochem Cell Biol. 2001 Jan;33(1):95-102. doi: 10.1016/s1357-2725(00)00050-9.

Abstract

A mannose- and glucose-binding lectin bearing considerable sequence similarity to other legume lectins was isolated using a simple procedure, from legumes of the sugar snap Pisum sativum var. macrocarpon. The lectin was unadsorbed on Affi-gel blue gel and Q-Sepharose in 10 mM Tris-HCl buffer (pH 7.2) and adsorbed on SP-Toyopearl in 50 mM NaOAc buffer (pH 5). An albumin could also be purified at the same time. It was unadsorbed on Affi-gel Blue gel, adsorbed on Q-Sepharose and unadsorbed on SP-Toyopearl under the aforementioned chromatographic conditions. The lectin was almost identical in N-terminal sequences of its alpha- and beta-subunit to lectin from P. sativum L. var. Feltham First except for the 19th N-terminal residue of the beta-subunit. The lectin was devoid of antifungal activity. Out of the 15 N-terminal amino acids examined in pea albumin, three were different between the two varieties of P. sativum.

MeSH terms

  • Albumins / chemistry*
  • Albumins / isolation & purification*
  • Amino Acid Sequence
  • Chromatography, Agarose
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Hemagglutinins / metabolism
  • Lectins / antagonists & inhibitors
  • Lectins / chemistry*
  • Lectins / isolation & purification*
  • Molecular Sequence Data
  • Pisum sativum / chemistry*
  • Plant Lectins
  • RNA, Messenger / metabolism
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • Albumins
  • Hemagglutinins
  • Lectins
  • Plant Lectins
  • RNA, Messenger