Mannose-binding lectin fromCurcuma zedoaria Rosc

Tipthara, Ponpimol; Sangvanich, Polkit; Macth, Marcus; Petsom, Amorn

doi:10.1007/bf03030626

Cited by 9 publications

(6 citation statements)

References 20 publications

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“…Note, however, that the predicted (theoretical) mass of the homologous proteins used to identify these three spots are slightly higher for A27 and A34 (19.5 and 20.3 kDa, respectively) but significantly so for A20 with a predicted mass of 404 kDa. A mannose binding lectin with a molecular mass of 13.4 kDa was also isolated from C. zedoary [ 39 ]. In addition, six homologous lectin proteins of various molecular masses (8.84-32.8 kDa) were found in C. aromatica [ 40 ].…”

Section: Resultsmentioning

confidence: 99%

A proteomic analysis of Curcuma comosa Roxb. rhizomes

et al. 2011

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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.

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Section: Resultsmentioning

confidence: 99%

A proteomic analysis of Curcuma comosa Roxb. rhizomes

et al. 2011

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“…However, despite the widespread usage of members of this general for medical applications, reports of lectins from Curcuma plants are scarce. A mannose-binding lectin from the Zingiberaceae member, Curcuma zedoaria Rosc., has been identified and found to have sequence similarity to a mannose-binding lectin from the broad-leaved helleborine orchid, Epipactis helleborine (L) Crantz (Asparageles: Orchidaceae) [27]. In the related Curcuma aromatica, six putative proteins from nine bands derived from a rhizome preparation showed similarity with other lectin sequences [28], whilst a study on the hemagglutinating activity of Curcuma plants found hemagglutinating activity in the species of this study, Khamindum or Curcuma amarissima [29].…”

Section: Introductionmentioning

confidence: 94%

Antifungal and Antiproliferative Activities of Lectin from the Rhizomes of Curcuma amarissima Roscoe

Kheeree

Sangvanich

Puthong

et al. 2009

Appl Biochem Biotechnol

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A lectin was purified from the rhizomes of Curcuma amarissima Roscoe by aqueous extraction, fractionation with 80% saturated ammonium sulfate, and a combination of affinity and gel chromatography on ConA Sepharose and Superdex G-75, respectively. The molecular mass of the purified lectin was 32.4 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The lectin showed no significant specificity in its ability to hemagglutinate erythrocytes from human blood groups (A, B, AB, and O), but for other animals, it only agglutinated rabbit and rat, and not mouse, guinea pig, goose, and sheep erythrocytes. The lectin was stable at temperatures below 40 degrees C, but the hemagglutinating activity halved when it was heated to 45-85 degrees C and was completely lost at 95 degrees C. The hemagglutinating activity was more stable at 80 degrees C than at 70 degrees C and was rapidly inactivated at 90 degrees C. It showed a maximum hemagglutination activity within the pH range of 8.0-11.0. The deduced amino acid sequence of an internal tryptic peptide sequence of this purified lectin showed sequence similarity (homology) to other members of the leucoagglutinating phytohemagglutinin precursor family, whilst the complete lectin inhibited the in vitro growth of three plant pathogenic fungi, Fusarium oxysporum, Exserohilum turicicum, and Colectrotrichum cassiicola, at a concentration of 17.5 to 35 microg, and showed in vitro cytotoxicity against the BT474 breast cancer cell line with an IC(50) of approximately 21.2 microg.

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“…The purification process was slightly modified from the method described by Tipthara [24] in that Tris-HCl buffer pH 7.2 and an SP sepharose (Amersham Pharmacia Biotech, UK) column were used instead. Briefly, 100 mg of crude protein powder was dissolved in 10 ml of 20 mM Tris-HCl buffer pH 7.2.…”

Section: Extraction Of Protein From the Rhizomes Of Z Ottensiimentioning

confidence: 99%

A Novel α-Glucosidase Inhibitor Protein from the Rhizomes of Zingiber ottensii Valeton

Tiengburanatam

Boonmee

Sangvanich

et al. 2010

Appl Biochem Biotechnol

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The objective of this study was to investigate a new protein with α-glucosidase inhibitory activity from the rhizomes of Zingiber ottensii. With a simple salting-out technique followed by single-step anion-exchange purification, the protein was successfully purified from the rhizomes. This protein was found to have three likely sub-unit types, 32.5, 15.2, and 13.8 kDa, as revealed by native and reducing SDS-PAGE analysis. Determination of the kinetics of the inhibition of α-glucosidase from Saccharomyces cerevisiae by standard enzymatic methods indicated the maximum percent inhibition; IC(50) and K ( i ) of this protein were 77.5%, 30.15 μg/ml, and 140 μmol, while the K ( m ) and V ( max ) were 2.35 μmol and 0.11 mM/min, respectively. The inhibitory action was pH-independent within the pH range 2-10, but was potentially affected by buffer salts, and was relatively temperature-stable between 4-35 °C, with a maximum activity at 65 °C. The amino acid sequence of an internal fragment of this purified Z. ottensii rhizomal protein had a similarity to the sequence from the plant cysteine proteinase family. Although this α-glucosidase inhibitory protein was purified from Z. ottensii rhizomes and preliminarily characterized, further studies are needed prior to firm applications being envisaged.

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Mannose-binding lectin fromCurcuma zedoaria Rosc

Cited by 9 publications

References 20 publications

A proteomic analysis of Curcuma comosa Roxb. rhizomes

A proteomic analysis of Curcuma comosa Roxb. rhizomes

Antifungal and Antiproliferative Activities of Lectin from the Rhizomes of Curcuma amarissima Roscoe

A Novel α-Glucosidase Inhibitor Protein from the Rhizomes of Zingiber ottensii Valeton

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