Purification and characterization of a small (7.3 kDa) putative lipid transfer protein from maize seeds

• Published in: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Vol. 794; no. 1; pp. 109 - 114
• Main Authors: Castro, Mariana S., Gerhardt, Isabel R., Orrù, Stefania, Pucci, Piero, Bloch, Carlos
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 25.08.2003; Elsevier Science
• Subjects: Amino Acid Sequence; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Antigens, Plant; Biological and medical sciences; Carrier Proteins - chemistry; Carrier Proteins - isolation & purification; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Lipid transfer proteins; Molecular Sequence Data; Plant Proteins; Proteins; Seeds - chemistry; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Zea mays - embryology; Characterization; Lipid transfer proteins; Purification; Seeds; Serine endopeptidases; Enzyme; Corn; Lipids; Electrospray; Protein; Peptidases; Trypsin; Ionization; Plant origin; Transfer; Hydrolases; Mass spectrometry
• ISSN: 1570-0232; 1873-376X
• DOI: 10.1016/S1570-0232(03)00423-9

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.