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EnglishThe 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.
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| Titolo: | Purification and characterization of a small (7.3 kDa) putative lipid transfer protein from maize seeds. | |
| Autori: | ||
| Data di pubblicazione: | 2003 | |
| Rivista: | ||
| Abstract: | 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. | |
| Handle: | http://hdl.handle.net/11367/31421 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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|---|---|---|---|---|
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http://hdl.handle.net/11367/31421
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