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Purification and Primary Structure of Novel Lipid Transfer Proteins from Germinated Lentil (Lens culinaris) Seeds


E. I. Finkina1, S. V. Balandin1, M. V. Serebryakova2, N. A. Potapenko1, A. A. Tagaev1, and T. V. Ovchinnikova1*

1Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (495) 336-4333; E-mail: ovch@ibch.ru

2Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, ul. Pogodinskaya 10, 119121 Moscow, Russia; fax: (495) 245-0857

* To whom correspondence should be addressed.

Received November 23, 2006; Revision received December 18, 2006
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

DOI: 10.1134/S0006297907040104