Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa).
A novel 7-kDa non-specific lipid transfer protein-2 (nsLTP2) has been isolated from rice (Oryza sativa) seeds. In contrast to nsLTP1s, few nsLTP2s have been purified and characterized. Complete amino acid sequence of rice nsLTP2 was determined by N-terminal Edman degradation of the intact protein as well as the peptide fragments resulted from trypsin digestions. Rice nsLTP2 consists of 69 amino acid residues with eight conserved cysteines forming four disulfide bonds. The secondary structure of rice nsLTP2 is predominantly alpha-helical as determined by circular dichroism spectroscopy. Cysteine pairings of nsLTP2 have one miss match at Cys(35)-X-Cys(37) motif compared to nsLTP1. Primary structure analysis of various plant nsLTP2s revealed an interesting conservation of sequence features among nsLTP2 family.
Liu
Yaw-Jen
YJ
Department of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan, ROC.
Samuel
Dharmaraj
D
Lin
Chi-Hung
CH
Lyu
Ping-Chiang
PC
D000595:Amino Acid Sequence; D050356:Lipid Metabolism; D026901:Membrane Transport Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D012275:Oryza / Q000378:metabolism*; D010940:Plant Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D016415:Sequence Alignment
D026901:Membrane Transport Proteins; D010940:Plant Proteins