Hemagglutinating activity and corresponding putative sequence identity from <i>Curcuma aromatica</i> rhizome

Tiptara, Ponpimol; Petsom, Amorn; Roengsumran, Sophon; Sangvanich, Polkit

doi:10.1002/jsfa.3184

Cited by 12 publications

(6 citation statements)

References 23 publications

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“…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 ]. Most of them are mannose binding lectins.…”

Section: Resultsmentioning

confidence: 99%

“…Most plant cysteine proteases belong to the papain and legumain families. Recently this enzyme family was reported from three members of the ginger family, in C. longa [ 43 ], C. aromatica [ 40 ] and Z. offinale Roscoe [ 44 ], and this ginger protease is used as a food improver and anti-inflammatory agent. Founding cysteine protease in four members of Zingiberaceae plant, C. comosa, C. longa, C. aromatica and Z. offinale at difference molecular weigh and pI position, the ginger cysteine protease might be a protein marker to classify specific species in this family in the future.…”

Section: Resultsmentioning

confidence: 99%

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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%

Section: Resultsmentioning

confidence: 99%

A proteomic analysis of Curcuma comosa Roxb. rhizomes

et al. 2011

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“…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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“…Protein was isolated from the rhizomes using the procedure described by Tiptara [22] and Samarkina [23] with some modification. Briefly, the rhizomes were peeled, minced into small cubes (about 5×5×5 mm), and soaked in 20 mM Tris-HCl buffer pH 7.2, containing 0.15 M NaCl, with care to cause minimal oxidation by air exposure.…”

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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Hemagglutinating activity and corresponding putative sequence identity from Curcuma aromatica rhizome

Cited by 12 publications

References 23 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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