4.2 Article

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

Journal

BIOCHEMISTRY-MOSCOW
Volume 72, Issue 4, Pages 430-438

Publisher

MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0006297907040104

Keywords

lipid transfer proteins; lentil; germinated seeds; primary structure; antibacterial activity; cDNA

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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.

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