Biochemistry (Moscow)

, Volume 72, Issue 4, pp 430–438 | Cite as

Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds

  • E. I. Finkina
  • S. V. Balandin
  • M. V. Serebryakova
  • N. A. Potapenko
  • A. A. Tagaev
  • T. V. Ovchinnikova


A subfamily of eight novel lipid transfer proteins designated as Lc-LTP1-8 was found in the lentil Lens culinaris. Lc-LTP2, Lc-LTP4, Lc-LTP7, and Lc-LTP8 were purified from germinated lentil seeds, and their molecular masses (9268.7, 9282.7, 9121.5, 9135.5 daltons) and complete amino acid sequences were determined. The purified proteins consist of 92–93 amino acid residues, have four disulfide bonds, and inhibit growth of Agrobacterium tumefaciens. Total RNA was isolated from germinated lentil seeds, RT-PCR and cloning were performed, and the cDNAs of six LTPs were sequenced. Precursor 116–118-residue proteins with 24–25-residue signal peptides were found, and two of them are purified proteins Lc-LTP2 and Lc-LTP4.

Key words

lipid transfer proteins lentil germinated seeds primary structure antibacterial activity cDNA 



fast protein liquid chromatography


lipid transfer protein


matrix-assisted laser desorption ionization time-of-flight mass spectrometry


pathogenesis-related proteins


rapid amplification of cDNA ends


reverse trnascription polymerase chain reaction


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Copyright information

© Pleiades Publishing, Ltd. 2007

Authors and Affiliations

  • E. I. Finkina
    • 1
  • S. V. Balandin
    • 1
  • M. V. Serebryakova
    • 2
  • N. A. Potapenko
    • 1
  • A. A. Tagaev
    • 1
  • T. V. Ovchinnikova
    • 1
  1. 1.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia
  2. 2.Orekhovich Institute of Biomedical ChemistryRussian Academy of Medical SciencesMoscowRussia

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