Purification and characterization of a small (7.3 kDa) putative lipid transfer protein from maize seeds.
The present study reports, for the first time in literature, the purification and biochemical characterization of a small basic protein from maize seeds similar to plant lipid transfer proteins-2, named mLTP2. The mLTP2 consists of 70 amino acid residues and has an M(r) of 7303.83, determined by electrospray ionization mass spectrometry. The primary structure of mLTP2 was determined by automated Edman degradation of the intact protein and peptides obtained from digestions with trypsin and by C-terminal sequencing using carboxypeptidase Y. The mLTP2 exhibits high sequence similarity (51-44% identical positions) with other plant LTP2s previously described.
Castro
Mariana S
MS
Departamento de Ciências Fisiológicas/IB, Universidade de Brasília, 70.910-900, Brasília/DF, Brazil. mcastro@unb.br
Gerhardt
Isabel R
IR
Orrù
Stefania
S
Pucci
Piero
P
Bloch
Carlos
C
D000595:Amino Acid Sequence; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010940:Plant Proteins; D012639:Seeds / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D021241:Spectrometry, Mass, Electrospray Ionization; D003313:Zea mays / Q000196:embryology*
D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant