Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds
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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.
Key wordslipid 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
rapid amplification of cDNA ends
reverse trnascription polymerase chain reaction
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