WordNet

a liquid solution that results from elution
that is flowing outward (同)outflowing
water mixed with waste matter (同)wastewater, sewer water

PrepTutorEJDIC

流出物,廃水;(湖・貯水池などからの)放流

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/03/06 22:25:57」(JST)

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Chromatography column

Elution is a term used in analytical and organic chemistry to describe the process of extracting one material from another by washing with a solvent (as in washing of loaded ion-exchange resins to remove captured ions).

In a liquid chromatography experiment, for example, an analyte is generally adsorbed, or "bound to", an adsorbent in a liquid chromatography column. The adsorbent, a solid phase (stationary phase), is a powder which is coated onto a solid support. Based on an adsorbent's composition, it can have varying affinities to "hold" onto other molecules—forming a thin film on its outside surface (or on its internal surface if there are cavities within the compound). Elution then is the process of removing analytes from the adsorbent by running a solvent, called an "eluent", past the adsorbent/analyte complex. As the solvent molecules "elute", or travel down through the chromatography column, they can either pass by the adsorbent/analyte complex or they can displace the analyte by binding to the adsorbent in its place. After the solvent molecules displace the analyte, the analyte can be carried out of the column for analysis. This is why as the mobile phase passes out of the column, it typically flows into a detector or is collected for compositional analysis.

Predicting and controlling the order of elution is a key aspect of column chromatographic methods.

Eluotropic Series

An eluotropic series is listing of various compounds in order of eluting power for a given adsorbent. The “eluting power” of a solvent is largely a measure of how well the solvent can "pull" an analyte off the adsorbent to which it is attached. This often happens when the eluent adsorbs onto the stationary phase, displacing the analyte. Such series are useful for determining necessary solvents needed for chromatography of chemical compounds. Normally such a series progresses from non-polar solvents, such as n-hexane, to polar solvents such as methanol or water. The order of solvents in an eluotropic series depends both on the stationary phase as well as on the compound used to determine the order.

Adsorption Strength (Least Strongly Adsorbed -> Most Strongly Adsorbed)
Saturated hydrocarbons; alkyl halides	Unsaturated hydrocarbons; Alkenyl Halides	Aromatic Hydrocarbons; Aryl Halides	Polyhalogenated Hydrocarbons	Ethers	Esters	Aldehydes and Ketones	Alcohols	Acids and Bases (Amines)

Eluting Power (Least Eluting Power -> Greatest Eluting Power)
Hexane or Pentane	Cyclohexane	Benzene	Dichloromethane	Chloroform	Ether (anhydrous)	Ethyl Acetate (anhydrous)	Acetone (anhydrous)	Ethanol	Methanol	Water	Pyridine	Acetic Acid

Eluent

The eluent is the "carrier" portion of the mobile phase. It moves the analytes through the chromatograph. In liquid chromatography, the eluent is the liquid solvent; in gas chromatography, it is the carrier gas.^[1]

Eluate

The analyte material that emerge from the chromatograph. It specifically includes both the analytes and solutes passing through the column, while the eluent is only the carrier.

Elution Time and Elution Volume

The elution time of a solute is the time between the start of the separation (the time at which the solute enters the column) and the time at which the solute elutes. In the same way, the elution volume is the volume of eluent required to cause elution. Under standard conditions for a known mix of solutes in a certain technique, the elution volume may be enough information to identify solutes. For instance, a mixture of amino acids may be separated by ion-exchange chromatography. Under a particular set of conditions, the amino acids will elute in the same order and at the same elution volume.

References

^ "IUPAC Gold Book: eluent". International Union of Pure and Applied Chemistry. http://goldbook.iupac.org/E02040.html. Retrieved 2008-09-28.

Brown, Phillis (2001). Advances in chromatography. CRC Press. pp. 36. ISBN 0-8247-0509-2.

External links

Chemistry glossary
Eluotropic series

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English Journal

Hagfish C1q: Its unique binding property.

Yamaguchi T1, Takamune K2, Kondo M3, Takahashi Y3, Kato-Unoki Y4, Nakao M4, Sano N5, Fujii T5.Author information 1Department of Biological Science, Graduate School of Science and Technology, Kumamoto University, 2-39-1 Kurokami, Kumamoto 860-8555, Japan.2Department of Biological Science, Graduate School of Science and Technology, Kumamoto University, 2-39-1 Kurokami, Kumamoto 860-8555, Japan. Electronic address: takamune@gpo.kumamoto-u.ac.jp.3Department of Applied Aquabiology, National Fisheries University, Shimonoseki, Yamaguchi 759-6595, Japan.4Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka 812-8581, Japan.5Department of Health Sciences, Faculty of Human Culture and Science, Prefectural University of Hiroshima, Ujina-Higashi, Hiroshima 734-8558, Japan.AbstractHagfish C1q (HaC1q) was identified and characterized as a pattern-recognition molecule (PRM) in the hagfish complement system. The serum from hagfish, Eptatretus burgeri, was applied to a GlcNAc-agarose column and eluted sequentially with GlcNAc and EDTA. Four (31, 27, 26, and 19kDa) and one (26kDa) proteins were detected as bound molecules in the GlcNAc- and the EDTA-eluates, respectively. Among these, the 26kDa protein from the EDTA eluate was found to be a homologue of mammalian C1q through cDNA analysis. HaC1q had an ability to bind to various microbes in a Ca(2+)-dependent manner and its target ligands on the microbes were lipopolysaccharide, lipoteichoic acid, and peptidoglycan. The binding of HaC1q to GlcNAc-agarose was not inhibited by an excess amount of monosaccharide such as GlcNAc. While HaC1q bound to Sepharose 6B with a matrix of GlcNAc-agarose (polymer of agarobiose), it did not bind to Sepharose 4B that contained lower concentration of agarobiose than Sepharose 6B. Therefore, the target of HaC1q on GlcNAc-agarose was concluded to be agarobiose and high density of the target moiety seemed to be required for the stable binding. This finding was in accordance with the known behavior of other lectins involved in the complement system. We have concluded that HaC1q recognizes agarobiose-like structures present on the surface of microbes and acts as a pattern-recognition molecule in the process for elimination of invading microbes.
Developmental and comparative immunology.Dev Comp Immunol.2014 Mar;43(1):47-53. doi: 10.1016/j.dci.2013.10.009. Epub 2013 Nov 4.
Hagfish C1q (HaC1q) was identified and characterized as a pattern-recognition molecule (PRM) in the hagfish complement system. The serum from hagfish, Eptatretus burgeri, was applied to a GlcNAc-agarose column and eluted sequentially with GlcNAc and EDTA. Four (31, 27, 26, and 19kDa) and one (26kDa)
PMID 24201131

Liquid chromatography-tandem mass spectrometric assay for the PARP inhibitor rucaparib in plasma.

Sparidans RW, Durmus S, Schinkel AH, Schellens JH, Beijnen JH.Author information Utrecht University, Faculty of Science, Department of Pharmaceutical Sciences, Division of Pharmacoepidemiology & Clinical Pharmacology, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands. Electronic address: R.W.Sparidans@uu.nl.AbstractA quantitative bioanalytical liquid chromatography-tandem mass spectrometric (LC-MS/MS) assay for the poly(ADP-ribose) polymerase-1 inhibitor rucaparib was developed and validated. Plasma samples were pre-treated using protein precipitation with acetonitrile containing gefitinib as internal standard. Diluted extract was directly injected into the reversed-phase chromatographic system. The eluate was transferred into the electrospray interface with positive ionization and the analyte was detected in the selected reaction monitoring mode of a triple quadrupole mass spectrometer. The assay was validated in a 1.25-2000ng/ml calibration range with r(2)=0.9958±0.0012 for linear regression with quadratic weighting (n=6). Within day precisions (n=18) were 2.0-5.4%, between day (3 days; n=18) precisions 3.2-8.0% and accuracies (n=18) were 89.7-93.2%. At the lower limit of quantification (1.25ng/ml) these parameters were 9.6%, 13.7% and 85.3%, respectively. The drug was sufficiently stable under all relevant analytical conditions. Finally, the assay was successfully used to determine drug pharmacokinetics in female FVB wild type mice.
Journal of pharmaceutical and biomedical analysis.J Pharm Biomed Anal.2014 Jan 25;88:626-9. doi: 10.1016/j.jpba.2013.10.016. Epub 2013 Oct 23.
A quantitative bioanalytical liquid chromatography-tandem mass spectrometric (LC-MS/MS) assay for the poly(ADP-ribose) polymerase-1 inhibitor rucaparib was developed and validated. Plasma samples were pre-treated using protein precipitation with acetonitrile containing gefitinib as internal standard
PMID 24216281

How to address the sample preparation of hydrophilic compounds: Determination of entecavir in plasma and plasma ultrafiltrate with novel extraction sorbents.

Vlčková H, Janák J, Gottvald T, Trejtnar F, Solich P, Nováková L.Author information Department of Analytical Chemistry, Faculty of Pharmacy, Charles University in Prague, Heyrovského 1203, 500 05 Hradec Králové, Czech Republic.AbstractTwo fast, simple, selective and economical sample preparation methods for the determination of entecavir in biological materials available at low amounts are reported. The choice of optimal extraction techniques was performed with regard to analyte hydrophilicity, sample volumes, selectivity, method recovery and rapidity. The compatibility of the eluate with the hydrophilic interaction chromatography (HILIC) mobile phase was crucial to allow the elimination of the evaporation and reconstitution steps and to obtain acceptable peak shapes. Different types of sorbents were employed for the extraction of two biological materials (plasma and plasma ultrafiltrate). The mixed-mode polymeric sorbent MCX was chosen as a suitable one for the solid phase extraction (SPE) of plasma samples. The analytes were eluted with 1ml of the mixture of 5 % ammonium hydroxide in ACN:water (95:5). Protein precipitation (PP) with 1ml of ACN was used to remove proteins from 500μl of plasma sample prior to SPE extraction. The microextraction by packed sorbent (MEPS) was employed for the cleaning up of plasma ultrafiltrate samples due to very small volumes available for the analysis. MEPS implemented a novel sorbent based on porous graphitic carbon, semi-automatic analytical syringe and a small volume of sample (50μl). The elution step was performed using 100μl of the mixture of 5mM ammonium acetate pH 4.0:ACN (25:75). The MEPS eluate was fully compatible with HILIC mobile phase subsequently used for the analysis of entecavir, unlike SPE eluate, which had to be evaporated and reconstituted in mobile phase. Both analytical methods were validated and demonstrated good linearity in a range 1-100ng/ml (r(2)>0.9992) for plasma samples and in a range 0.5-100ng/ml (0.9991) for the plasma ultrafiltrate samples. Intra-day accuracy expressed as recovery was within the range from 80-98% for the plasma samples and 97-106% for the plasma ultrafiltrate samples. Inter-day accuracy ranged within 81-106% for the plasma and 95-101% for the plasma ultrafiltrate samples. The intra-day precision expressed as the % of RSD was lower than 4% for both matrices and inter-day precision was lower than 7% for plasma and lower than 17% for plasma ultrafiltrate. Method sensitivity reached LLOQ of 1ng/ml in plasma and 0.5ng/ml in plasma ultrafiltrate samples. The method was applied for the determination of concentration-time profiles of entecavir in plasma of the perfusate for rat kidney perfusion and for the measurement of concentration of entecavir in plasma ultrafiltrate samples. The results should be helpful in the evaluation of excretion mechanism of entecavir.
Journal of pharmaceutical and biomedical analysis.J Pharm Biomed Anal.2014 Jan 25;88:337-44. doi: 10.1016/j.jpba.2013.08.034. Epub 2013 Sep 2.
Two fast, simple, selective and economical sample preparation methods for the determination of entecavir in biological materials available at low amounts are reported. The choice of optimal extraction techniques was performed with regard to analyte hydrophilicity, sample volumes, selectivity, method
PMID 24126184

Japanese Journal

P-59 S-PRGフィラー溶出液に浸漬したヒト歯質中ホウ素の^<11>B-NMRによる構造解析(コンポジットレジン,一般講演(ポスター発表),第62回日本歯科理工学会学術講演会)

和田敬広,本郷敏雄,宇尾基弘
日本歯科理工学会誌 32(5), 409, 2013-09-25
… Enamel and dentin powders were immersed in S-PRG filler eluate (B=600 ppm) for about 1 year. …
NAID 110009674296

Rapid Single-Stage Separation of Micrometer-Long and High-Purity Semiconducting Carbon Nanotubes by Gel Filtration

Thendie Boanerges,Miyata Yasumitsu,Kitaura Ryo,Miyauchi Yuhei,Matsuda Kazunari,Shinohara Hisanori
Applied Physics Express 6(6), 065101-065101-4, 2013-06-25
… These differences allow the separation of length-sorted and purity-enhanced s-SWCNTs by fractionated collection of the eluate, which provides the desired nanotubes for electronic device applications. …
NAID 150000107133

下水処理場における放射性セシウムの挙動調査および溶出試験

對馬育夫,小越眞佐司,山下洋正 [他],原田一郎
水環境学会誌 36(1), 23-28, 2013
… Results indicate that the radioactivity of the eluate from 9 out of 12 samples was undetectable; …
NAID 130003368712