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Characterization and Biological Activities of Lectin Isolated from Pinellia Ternata

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Characterization and Biological Activities of Lectin Isolated from Pinellia Ternata Advances in Biological Chemistry, 2012, 2, 115-122 ABC http://dx.doi.org/10.4236/abc.2012.22014 Published Online May 2012 (http://www.SciRP.org/journal/abc/) Characterization and biological activities of lectin isolated from Pinellia ternata Ruijuan Feng, Weibiao Zhang, Tao Xu* Institute of Bioengineering, Zhejiang Sci-Tech University, Hangzhou, China Email: *[email protected] Received 16 February 2012; revised 15 March 2012; accepted 25 March 2012 ABSTRACT which are from the major plant lectin families that have been reported. Up to now,no standard methods for plant In this paper, Pinellia ternata lectin (PTL) purified lectins extraction has been established. Generally, the from 95% saturated ammonium sulfate precipitation aqueous buffer method is used for the extration of it, and by applying mannose-Sepharose 4B affinity column the buffer including distilled water, normal saline, dilute chromatography was first described. The mannose- acid, PBS and so on. The lowest effect extraction method Sepharose 4B affinity adsorption gel has already been is the distilled water method [3]. None fixed method for designed and prepared before the experiments ac- plant agglutinin purification and the costless and the cording the combinative characterization between most convenient method is salting out method, the prin- lectin and mannose. Mass spectrometry analysis re- cipal is that different protein has different solubility in sult shows that PTL is a glycoprotein with the mo- different concentrations of saline solution and proteins lecular weight of 12.165 kD. It was conclude that PTL can be precipitated in different saturation saline solution, had strong agglutination effects on mouse red blood thus proteins was separated. (NH ) SO fractional preci- cells, and the minimum reaction concentration was 25 4 2 4 pitation method was often used in the extraction of plant μg/ml according the Hemagglutination. Results of lectins, because of its large solubility and small tem- automatic amino acid analysis indicated that PTL perature coefficient in water, but the purified protein mainly contained 15 varieties of amino acids, of which cannot be obtained. The last method is most commonly the minimum content was cysteine and aspartate was used in biological chemical separation, purification and the maximum. Cell experiment results suggested that identification of biological macromolecules: chromato- PTL of low concentrations (0.004 mg/ml, 0.02 mg/ml graphy. According to the principles of chromatography, and 0.1 mg/ml) promoted HeLa cell proliferation, but there are three methods are used commonly: affinity chro- the effect weakened with the concentrations and matography (specific ligand-Sepharose, porcine thyroid treated-time increasing. However, the HeLa cells pro- globulin affinity chromatography), ion exchange chroma- liferation was intensively inhibited by higher PTL tography (anion exchange chromatography DEAE-Se- concentrations (0.5 mg/ml and 1 mg/ml), and the ef- pharose, cation exchange chromatography CM-Sepha- fect increased in a dose and time dependent manner. rose) and molecular sieve chromatography (Sephadex, Sephacry). In order to achieve better separation effect, Keywords: Pinellia ternata Lectin; Mannose-Sepharose two or three kinds of different methods were often used 4B Affinity Chromatography; Glycoprotein; Hela Cell; together [4-8]. Separation and purification effect of the MTT Method samples are also assessed by methods such as SDS- PAGE or HPLC. 1. INTRODUCTION Pinellia ternata (Thunb.) Breit., a traditional Chinese medicinal herb belongings to family Araceae [9], has Plant lectins or agglutinins, widely distributed in higher been characterized as pungent, warm in nature, and toxic plant, are considered as an extended group of proteins, and was firstly recorded in Shen Nong Ben Cao Jing. The which according to a recently updated definition, com- main ingredients of which are starch, protein, pinellin, prise all plant proteins possessing at least one non- alkaloids, polysaccharides, amino acids, volatile oil, catalytic domain that binds reversibly to specific mono- organic acids, sterols, flavonoids, tannins and other or oligosaccharides (glycoconjugate) [1,2]. One group of chemical compositions [10]. Pinellia ternata (Thunb.) lectins is the so-called monocot mannose-binding lectin Breit has pharmacological functions of terminating early *Corresponding author. pregnancy, anti-tumor, anti-arrhythmic, anti-ulcer, lower- OPEN ACCESS 116 R. J. Feng et al. / Advances in Biological Chemistry 2 (2012) 115-122 ing blood pressure, sedative-hypnotic, antitussive and 2.2. Mannose-Sepharose 4B Affinity Gel anti-inflammatory role in detoxification [11,12]. P. ter- Preparation nata lectin (PTL) was a monocot mannose-bingding lectin and was demonstrated as the major contributor for Cleaning: Washing DMSO away from alkylene oxide its antitumor activity [13,14]. PTL has the ability of activated agarose gel preserved in 50% DMSO with control fungal pathogens through transgenic expression deionized water 10 to 20 times the volume of the gel, preferable alternative to toxic chemicals having serious then drained vacuum. ecological and social consequences has been proved. Coupling: 25 mg, 50 mg and 100 mg mannose was dissolved in 10 ml 0.1 M sodium carbonate buffer PTL was first isolated with (NH4)2SO4 precipitation and crystallization method by Tao, Z. J. etc. in nineteen solution (pH 9.0), separately. Then put them into the eighties [15]. One PTL which was speculated to be the drained activated gel, respectively. Couple 12 to 24 hr in same as Tao’s was attained by porcine thyroglobulin a shaker oscillates at 37˚C. After the reaction, the so- immobilized affinity column chromatography [16] and lution was transferred to the funnel, drained (collect the molecular weight was speculated to be about 44 kD filtrate for unconjugated mannose analysis and coupling from the Sephadex G100 chromatography column fil- ligand density calculation), activated gel solution was tration behavior. SDS-PAGE gel electrophoresis result washed by deionized water and then drained, three gra- showed that there was only one protein band with the dients of ligand density (H), (M), (L) gel were obtained. molecular weight of about 12 kD, so it can be infered Closing: Put the dry coupling gel into a 100 ml tri- that the PTL consisted of four subunits. Gel filtration re- angle bottle, added 30 ml 1 M ethanol amine solution, sults of PTL measured by SPHER OGELTM-TSK 2000 then reacted 4 hr at 37˚C stirring 120 × g. Then the solu- SW showed its molecular weight was 33 kD, proving tion was transferred to the funnel, drained. Finally, the that PTL and molecular sieve column with hydrophobic gel was washed with deionized water. interaction. Cleaning: The medium coupled mannose was washed PTL is a glycoprotein, having agglutination activity on by 5 times deionized water of the volum of the medium red blood cells and the nature of specific binding of (0.5 M NaCl acetate buffer solution (pH 4.0), deionized mannose. Based on the nature of the mannose specific water, 0.5 M NaCl boric acid-four sodium borate (pH 8.0) binding with PTL, the mannose-Sepharose 4B affinity and deionized water)sufficiently, then drained. gel was designed and the PTL was isolated successfully. Preservation: The product was preserved in 20% etha- Mass spectrometry was used to determine the precise nol solution at 4˚C. molecular weight and purity of the isolated PTL. Amino acid composition of the PTL was detected with a the 2.3. Isolation of PTL from P. ternata automatic amino acid analyzer L-8800 AAA system and the results was statisticed and classified. Detecting and Pinellia tuber was well grinded and soaked in 20% NaCl hemagglutinating experiments of the glycoprotein were for 24 hr. The aqueous solution was centrifuged at performed to identify the separated product. Meanwhile, 12,000 × g, 4˚C for 30 min. The precipitation was dis- its effect on the growth of Hela cells was studied solved in 20% NaCl and dialyzed to remove (NH4)2SO4. preliminarily. These experiments were the groundwork Centrifuging and discarding the insoluble substance, then for the further study of PTL isolation and its phar- the supernatant was the rough product. macological mechanism. Mannose-Sepharose 4B affinity chromatographic co- The PTL subunits isolated and purificated by man- umn saturated with 20% NaCl was used to isolate PTL nose-Sepharose 4B affinity chromatography was first from the rough product. Adsorbed PTL was eluted with reported in this paper and its coagulation activity, gly- elution buffer (0.2 M mannose solution and 0.9% NaCl coprotein nature and amino acid composition were solution, respectively). The eluting sample was concen- detected. Further more, the anti-tumor activity of it on trated with Minitan Ultra Filtration System (Millipore, Hela cells was also studied. Molsheim, France), with a tangential flow decice on an 2. MATHERIALS AND METHODS ultra filtration membrane (cut-off 10,000 Da). The con- centrating sample was dialyzed against PBS buffer (pH 2.1. Materials 7.4). After dialysising, the sample was assessed by poly- Fresh Pinellia tuber was obtained from the Conservatory acrylamide gel electrophoresis (SDS-PAGE) in a slab gel of life of Biological Engineering Research Institute of system from Bio-Rad. SDS-PAGE was performed on Zhejiang Sci-Tech University and identified by associate 15% acrylamide gels. Also, we studied the effect on the professor Xu T. Experimental rats were purchased from separating efficiency of different equilibrium buffer Animal Center of Hangzhou Normal University. Hela (20% NaCl solution, 10% NaCl solution and PBS buffer) cells were reserved in our lab. and affinity gel of different ligand density. Copyright © 2012 SciRes. OPEN ACCESS R. J. Feng et al. / Advances in Biological Chemistry 2 (2012) 115-122 117 2.4. Partial Properties and Biological Activities tion, took photographs of cells treated by different con- of Isolated PTL centrations of PTL in different time under an inverted microscope. The molecular weight of PTL was determined with a PBSIIC mass spectrometer. NP20 chip calibration in- 3.
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