ロケット免疫電気泳動

WordNet

move back and forth or sideways; "the ship was rocking"; "the tall building swayed"; "She rocked back and forth on her feet" (同)sway, shake
material consisting of the aggregate of minerals like those making up the Earths crust; "that mountain is solid rock"; "stone is abundant in New England and there are many quarries" (同)stone
pitching dangerously to one side (同)careen, sway, tilt
a lump or mass of hard consolidated mineral matter; "he threw a rock at me" (同)stone
(figurative) someone who is strong and stable and dependable; "he was her rock during the crisis"; "Thou art Peter, and upon this rock I will build my church"--Gospel According to Matthew
cause to move back and forth; "rock the cradle"; "rock the baby"; "the wind swayed the trees gently" (同)sway
propel with a rocket
erect European annual often grown as a salad crop to be harvested when young and tender (同)roquette, garden rocket, rocket salad, arugula, Eruca sativa, Eruca vesicaria sativa
any vehicle self-propelled by a rocket engine (同)projectile
a jet engine containing its own propellant and driven by reaction propulsion (同)rocket engine
propels bright light high in the sky, or used to propel a lifesaving line or harpoon (同)skyrocket
shoot up abruptly, like a rocket; "prices skyrocketed" (同)skyrocket
electrophoresis to separate antigens and antibodies

PrepTutorEJDIC

〈U〉〈C〉『岩』,岩石;『岩壁』;《しばしば複数形で》岩礁 / 〈C〉『岩片』;《米話》『石』,小石 / 〈C〉岩のように強固(堅固)なもの,しっかりして頼りになるもの
(リズムをつけて)…‘を'『前後に』(『左右に』)『そっと揺り動かす』 / …‘を'『震動させる』,振動させる / 《話》…‘の'気を転倒させる,‘に'ショックを与える / 『前後に』(『左右に』)『そっと揺れ動く』 / 『震動する』,激しく揺れる / 揺れ / 動揺 / =rock'n'roll
『ロケット』;ロケット弾;ロケット推進ミサイル / 火矢;打ち上げ花火;のろし / 〈電車などが〉(ロケットのように)突進する / 〈値段などが〉急上昇する

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/06 10:24:00」(JST)

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Crossed immunoelectrophoresis of 2 microLitre of normal human serum. The electrophoresis was performed in thin layers of agarose, the pictured gel is about 5x8 cm. The lower part is the first dimension gel without antibodies, where the serum was applied into the slot at the lower left. The upper part is the second dimension gel with Dako antibodies against human serum proteins. More than 50 major serum proteins can be named.

Immunoelectrophoresis is a general name for a number of biochemical methods for separation and characterization of proteins based on electrophoresis and reaction with antibodies. All variants of immunoelectrophoresis require immunoglobulins, also known as antibodies reacting with the proteins to be separated or characterized. The methods were developed and used extensively during the second half of the 20th century. In somewhat chronological order: Immunoelectrophoretic analysis (one-dimensional immunoelectrophoresis ad modum Grabar), crossed immunoelectrophoresis (two-dimensional quantitative immunoelectrophoresis ad modum Clarke and Freeman or ad modum Laurell), rocket-immunoelectrophoresis (one-dimensional quantitative immunoelectrophoresis ad modum Laurell), fused rocket immunoelectrophoresis ad modum Svendsen and Harboe, affinity immunoelectrophoresis ad modum Bøg-Hansen.

Agarose as 1% gel slabs of about 1 mm thickness buffered at high pH (around 8.6) is traditionally preferred for the electrophoresis as well as the reaction with antibodies. The agarose was chosen as the gel matrix because it has large pores allowing free passage and separation of proteins, but provides an anchor for the immunoprecipitates of protein and specific antibodies. The high pH was chosen because antibodies are practically immobile at high pH. An electrophoresis equipment with a horizontal cooling plate was normally recommended for the electrophoresis.

Immunoprecipitates may be seen in the wet agarose gel, but are stained with protein stains like Coomassie Brilliant Blue in the dried gel. In contrast to SDS-gel electrophoresis, the electrophoresis in agarose allows native conditions, preserving the native structure and activities of the proteins under investigation, therefore immunoelectrophoresis allows characterization of enzyme activities and ligand binding etc. in addition to electrophoretic separation.

The immunoelectrophoretic analysis ad modum Grabar is the classical method of immunoelectrophoresis. Proteins are separated by electrophoresis, then antibodies are applied in a trough next to the separated proteins and immunoprecipitates are formed after a period of diffusion of the separated proteins and antibodies against each other. The introduction of the immunoelectrophoretic analysis gave a great boost to protein chemistry, some of the very first results were the resolution of proteins in biological fluids and biological extracts. Among the important observations made were the great number of different proteins in serum, the existence of several immunoglobulin classes and their electrophoretic heterogeneity.

Plasmodium Glutamate dehydrogenase (pGluDH) separated by Counterimmunoelectrophoresis^[1]

Crossed immunoelectrophoresis is also called two-dimensional quantitative immunoelectrophoresis ad modum Clarke and Freeman or ad modum Laurell. In this method the proteins are first separated during the first dimension electrophoresis, then instead of the diffusion towards the antibodies, the proteins are electrophoresed into an antibody-containing gel in the second dimension. Immunoprecipitation will take place during the second dimension electrophorsis and the immunoprecipitates have a characteristic bell-shape, each precipitate representing one antigen, the position of the precipitate being dependent on the amount of protein as well as the amount of specific antibody in the gel, so relative quantification can be performed. The sensitivity and resolving power of crossed immunoelectrophoresis is than that of the classical immunoelectrophoretic analysis and there are multiple variations of the technique useful for various purposes. Crossed immunoelectrophoresis has been used for studies of proteins in biological fluids, particularly human serum, and biological extracts.

Rocket immunoelectrophoresis is one-dimensional quantitative immunoelectrophoresis. The method has been used for quantitation of human serum proteins before automated methods became available.

Fused rocket immunoelectrophoresis is a modification of one-dimensional quantitative immunoelectrophorsis used for detailed measurement of proteins in fractions from protein separation experiments.

Affinity immunoelectrophoresis is based on changes in the electrophoretic pattern of proteins through specific interaction or complex formation with other macromolecules or ligands. Affinity immunoelectrophoresis has been used for estimation of binding constants, as for instance with lectins or for characterization of proteins with specific features like glycan content or ligand binding. Some variants of affinity immunoelectrophoresis are similar to affinity chromatography by use of immobilized ligands.

The open structure of the immunoprecipitate in the agarose gel will allow additional binding of radioactively labeled antibodies to reveal specific proteins. This variation has been used for identification of allergens through reaction with IgE.

Two factors determine that immunoelectrophoretic methods are not widely used. First they are rather work intensive and require some manual expertise. Second they require rather large amounts of polyclonal antibodies. Today gel electrophoresis followed by electroblotting is the preferred method for protein characterization because its ease of operation, its high sensitivity, and its low requirement for specific antibodies. In addition proteins are separated by gel electrophoresis on the basis of their apparent molecular weight, which is not accomplished by immunoelectrophoresis, but nevertheless immunoelectrophoretic methods are still useful when non-reducing conditions are needed.

References

^ Ling IT., Cooksley S., Bates PA., Hempelmann E., Wilson RJM. (1986). "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum". Parasitology 92 (2): 313–324. doi:10.1017/S0031182000064088. PMID 3086819.

External links

Comprehensive text edited by Niels H. Axelsen in Scandinavian Journal of Immunology, 1975 Volume 4 Supplement
Immunoelectrophoresis at the US National Library of Medicine Medical Subject Headings (MeSH)
http://www.lib.mcg.edu/edu/esimmuno/ch4/immelec.htm
Immuno-Electrophoresis. Immuno-Diffusion

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Activity and levels of factor XIII in a Venezuelan admixed population: association with rs5985 (Val35Leu) and STR F13A01 polymorphisms.

Vívenes M1, Castro de Guerra D, Rodríguez-Larralde A, Arocha-Piñango CL, Guerrero B.
Thrombosis research.Thromb Res.2012 Nov;130(5):729-34. doi: 10.1016/j.thromres.2012.07.027. Epub 2012 Aug 19.
INTRODUCTION: The single nucleotide polymorphism Val35Leu has been described within the A subunit of gene Factor XIII (FXIII-A) in association with an increase of FXIII activity. In the gene's promoter region STR F13A01 is present, however there is no available data related about its influence on th
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Transferrin changes in haemodialysed patients.

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