Purification and Characterization of a novel nsLTP from Oriza Sativa (rice)

         Lin CH(林祈宏), Samuel D(詹淼爾), Lo FC(羅鳳君), Liu YJ(劉耀禎),

    and Lyu PC(呂平江)

                   Department of Life Sciences, National Tsing Hua University, Hsinchu


Non-specific lipid transfer protein (nsLTP) is isolated from various plant sources including rice, wheat, barley and various fruits like apricot, grapes etc. LTP plays an important role in transferring lipid molecules between various lipid bilayers. Recently it has been reported to be the major allergene in fruits. nsLTPs consist of four helices tied together by four disulfide bonds forming a hydrophobic pocket. The hydrophobic pocket helps in binding and carrying hydrophobic molecules by LTP.  In this poster we report a novel form of non-specific lipid transfer protein(LTP2), which has been isolated from rice. LTP2 is a 68 amino acid protein (MW 7Kda) compared to 91 amino acids in LTP1 (MW 9Kda). The primary sequence of LTP2 shows 60% analogy with that of LTP1. LTP family has highly conserved cystines, but the disulfide pattern of LTP2 shows a mismatch. Secondary structure content of the LTP2 is similar to LTP1. The predominant α-helix structure is obvious from the circular dichroism (CD) measurement and the structure of LTP1 and LTP2 are compared by Nuclear Magnetic Resonance spectroscopy (NMR)