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

Mariana S. Castro, Isabel R. Gerhardt, Stefania Orrù, Piero Pucci, Carlos Bloch

Research output: Contribution to journalArticle

21 Citations (Scopus)

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 Mr 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.

Original languageEnglish
Pages (from-to)109-114
Number of pages6
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume794
Issue number1
DOIs
Publication statusPublished - Aug 25 2003

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Cathepsin A
Electrospray Ionization Mass Spectrometry
Trypsin
Proteolysis
Zea mays
Purification
Seed
Digestion
Seeds
Amino Acids
Electrospray ionization
Peptides
Mass spectrometry
Proteins
Degradation
plant LTP2 protein
lipid transfer protein

Keywords

  • Characterization
  • Lipid transfer proteins
  • Purification

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification and characterization of a small (7.3 kDa) putative lipid transfer protein from maize seeds. / Castro, Mariana S.; Gerhardt, Isabel R.; Orrù, Stefania; Pucci, Piero; Bloch, Carlos.

In: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, Vol. 794, No. 1, 25.08.2003, p. 109-114.

Research output: Contribution to journalArticle

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