Abstract
BackgroundThe similarly in plant physiology and the difficulty of plant classification, in some medicinal plant species, especially plants of the Zingiberaceae family, are a major problem for pharmacologists, leading to mistaken use. To overcome this problem, the proteomic base method was used to study protein profiles of the plant model, Curcuma comosa Roxb., which is a member of the Zingiberaceae and has been used in traditional Thai medicine as an anti-inflammatory agent for the treatment of postpartum uterine bleeding.ResultsDue to the complexity of protein extraction from this plant, microscale solution-phase isoelectric focusing (MicroSol-IEF) was used to enrich and improve the separation of Curcuma comosa rhizomes phenol-soluble proteins, prior to resolving and analyzing by two-dimensional polyacrylamide gel electrophoresis and identification by tandem mass spectrometry. The protein patterns showed a high abundance of protein spots in the acidic range, including three lectin proteins. The metabolic and defense enzymes, such as superoxide dismutase (SOD) and ascorbate peroxidase, that are associated with antioxidant activity, were mainly found in the basic region. Furthermore, cysteine protease was found in this plant, as had been previously reported in other Zingiberaceae plants.ConclusionThis report presents the protein profiles of the ginger plant, Curcuma comosa. Several interesting proteins were identified in this plant that may be used as a protein marker and aid in identifying plants of the Zingiberaceae family.
Highlights
The in plant physiology and the difficulty of plant classification, in some medicinal plant species, especially plants of the Zingiberaceae family, are a major problem for pharmacologists, leading to mistaken use
The biologically active proteins reported from Zingiberaceae plants include, antifungal proteins from Zingiber officinalis [11] and antioxidant proteins from C. longa [12] and C. zedoaria [13]
Their actual physiological functions are likely to be in the defense against phytophagous predators and phytopathogenic microorganisms [19,20]. These plant lectins have been found in a variety of plant species, including the ginger family where, for example, the mannose-binding lectin cDNA, Z. officinale agglutinin (ZOA) [21], was cloned from the rhizomes of Z
Summary
The in plant physiology and the difficulty of plant classification, in some medicinal plant species, especially plants of the Zingiberaceae family, are a major problem for pharmacologists, leading to mistaken use. The lectins or agglutinin proteins, a class of carbohydrate-binding non-immune origin proteins, have been used as tools in analytical biochemistry [14,15] including in medical applications, such as drug delivery [16], blood typing [17] and potential antineoplastic drugs [18], amongst others Their actual physiological functions are likely to be in the defense against phytophagous predators (mostly insects) and phytopathogenic microorganisms [19,20]. These plant lectins have been found in a variety of plant species, including the ginger family where, for example, the mannose-binding lectin cDNA, Z. officinale agglutinin (ZOA) [21], was cloned from the rhizomes of Z
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