HOME TheInfoList.com
Providing Lists of Related Topics to Help You Find Great Stuff
[::MainTopicLength::#1500] [::ListTopicLength::#1000] [::ListLength::#15] [::ListAdRepeat::#3]

Electrochromatography
Electrochromatography is a chemical separation technique in analytical chemistry, biochemistry and molecular biology used to resolve and separate mostly large biomolecules such as proteins. It is a combination of size exclusion chromatography (gel filtration chromatography) and gel electrophoresis. These separation mechanisms operate essentially in superposition along the length of a gel filtration column to which an axial electric field gradient has been added. The molecules are separated by size due to the gel filtration mechanism and by electrophoretic mobility due to the gel electrophoresis mechanism
[...More...]

"Electrochromatography" on:
Wikipedia
Google
Yahoo

picture info

Analytical Chemistry
Analytical chemistry
Analytical chemistry
studies and uses instruments and methods used to separate, identify, and quantify matter.[1] In practice separation, identification or quantification may constitute the entire analysis or be combined with another method. Separation isolates analytes. Qualitative analysis identifies analytes, while quantitative analysis determines the numerical amount or concentration. Analytical chemistry
Analytical chemistry
consists of classical, wet chemical methods and modern, instrumental methods.[2] Classical qualitative methods use separations such as precipitation, extraction, and distillation. Identification may be based on differences in color, odor, melting point, boiling point, radioactivity or reactivity. Classical quantitative analysis uses mass or volume changes to quantify amount. Instrumental methods may be used to separate samples using chromatography, electrophoresis or field flow fractionation
[...More...]

"Analytical Chemistry" on:
Wikipedia
Google
Yahoo

Electroosmosis
Electroosmotic flow (or electro-osmotic flow, often abbreviated EOF; synonymous with electroosmosis or electroendosmosis) is the motion of liquid induced by an applied potential across a porous material, capillary tube, membrane, microchannel, or any other fluid conduit. Because electroosmotic velocities are independent of conduit size, as long as the electrical double layer is much smaller than the characteristic length scale of the channel, electroosmotic flow will have little effect. Electroosmotic flow is most significant when in small channels
[...More...]

"Electroosmosis" on:
Wikipedia
Google
Yahoo

picture info

Electrophoresis
Electrophoresis
Electrophoresis
(from the Greek "Ηλεκτροφόρηση" meaning "to bear electrons") is the motion of dispersed particles relative to a fluid under the influence of a spatially uniform electric field.[1][2][3][4][5][6] This electrokinetic phenomenon was observed for the first time in 1807 by Russian professors Peter Ivanovich Strakhov and Ferdinand Frederic Reuss (Moscow State University),[7] who noticed that the application of a constant electric field caused clay particles dispersed in water to migrate. It is ultimately caused by the presence of a charged interface between the particle surface and the surrounding fluid
[...More...]

"Electrophoresis" on:
Wikipedia
Google
Yahoo

picture info

Biochemistry
Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms.[1] By controlling information flow through biochemical signaling and the flow of chemical energy through metabolism, biochemical processes give rise to the complexity of life
[...More...]

"Biochemistry" on:
Wikipedia
Google
Yahoo

picture info

International Standard Serial Number
An International Standard Serial Number
International Standard Serial Number
(ISSN) is an eight-digit serial number used to uniquely identify a serial publication.[1] The ISSN is especially helpful in distinguishing between serials with the same title. ISSN are used in ordering, cataloging, interlibrary loans, and other practices in connection with serial literature.[2] The ISSN system was first drafted as an International Organization for Standardization (ISO) international standard in 1971 and published as ISO 3297 in 1975.[3] ISO subcommittee TC 46/SC 9 is responsible for maintaining the standard. When a serial with the same content is published in more than one media type, a different ISSN is assigned to each media type. For example, many serials are published both in print and electronic media
[...More...]

"International Standard Serial Number" on:
Wikipedia
Google
Yahoo

picture info

Digital Object Identifier
In computing, a Digital Object Identifier or DOI is a persistent identifier or handle used to uniquely identify objects, standardized by the International Organization for Standardization
International Organization for Standardization
(ISO).[1] An implementation of the Handle System,[2][3] DOIs are in wide use mainly to identify academic, professional, and government information, such as journal articles, research reports and data sets, and official publications though they also have been used to identify other types of information resources, such as commercial videos. A DOI aims to be "resolvable", usually to some form of access to the information object to which the DOI refers. This is achieved by binding the DOI to metadata about the object, such as a URL, indicating where the object can be found. Thus, by being actionable and interoperable, a DOI differs from identifiers such as ISBNs and ISRCs which aim only to uniquely identify their referents
[...More...]

"Digital Object Identifier" on:
Wikipedia
Google
Yahoo

picture info

Two-dimensional Gel Electrophoresis
Two-dimensional gel electrophoresis, abbreviated as 2-DE or 2-D electrophoresis, is a form of gel electrophoresis commonly used to analyze proteins. Mixtures of proteins are separated by two properties in two dimensions on 2D gels. 2-DE was first independently introduced by O'Farrell[1] and Klose[2] in 1975.Contents1 Basis for separation 2 Detecting proteins 3 Common techniques3.1 IPG-DALT 3.2 IEF SDS-PAGE4 2D gel analysis software 5 See also 6 References 7 External linksBasis for separation[edit] 2-D electrophoresis begins with electrophoresis in the first dimension and then separates the molecules perpendicularly from the first to create an electropherogram in the second dimension. In electrophoresis in the first dimension, molecules are separated linearly according to their isoelectric point. In the second dimension, the molecules are then separated at 90 degrees from the first electropherogram according to molecular mass
[...More...]

"Two-dimensional Gel Electrophoresis" on:
Wikipedia
Google
Yahoo

picture info

Protein Electrophoresis
Protein
Protein
electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium: SDS polyacrylamide gel electrophoresis (in short: gel electrophoresis, PAGE, or SDS-electrophoresis), free-flow electrophoresis, electrofocusing, isotachophoresis, affinity electrophoresis, immunoelectrophoresis, counterelectrophoresis, and capillary electrophoresis. Each method has many variations with individual advantages and limitations. Gel electrophoresis
Gel electrophoresis
is often performed in combination with electroblotting immunoblotting to give additional information about a specific protein
[...More...]

"Protein Electrophoresis" on:
Wikipedia
Google
Yahoo

picture info

Immunoelectrophoresis
Immunoelectrophoresis
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
[...More...]

"Immunoelectrophoresis" on:
Wikipedia
Google
Yahoo

picture info

Molecular Biology
Molecular biology
Molecular biology
/məˈlɛkjʊlər/ is a branch of biochemistry which concerns the molecular basis of biological activity between biomolecules in the various systems of a cell, including the interactions between DNA, RNA, and proteins and their biosynthesis, as well as the regulation of these interactions.[1] Writing in Nature in 1961, William Astbury described molecular biology as:"...not so much a technique as an approach, an approach from the viewpoint of the so-called basic sciences with the leading idea of searching below the large-scale manifestations of classical biology for the corresponding molecular plan. It is concerned particularly with the forms of biological molecules and [...] is predominantly three-dimensional and structural—which does not mean, however, that it is merely a refinement of morphology
[...More...]

"Molecular Biology" on:
Wikipedia
Google
Yahoo

picture info

Electrophoretic Mobility
Electrophoresis
Electrophoresis
(from the Greek "Ηλεκτροφόρηση" meaning "to bear electrons") is the motion of dispersed particles relative to a fluid under the influence of a spatially uniform electric field.[1][2][3][4][5][6] This electrokinetic phenomenon was observed for the first time in 1807 by Russian professors Peter Ivanovich Strakhov and Ferdinand Frederic Reuss (Moscow State University),[7] who noticed that the application of a constant electric field caused clay particles dispersed in water to migrate. It is ultimately caused by the presence of a charged interface between the particle surface and the surrounding fluid
[...More...]

"Electrophoretic Mobility" on:
Wikipedia
Google
Yahoo

picture info

Biomolecule
A biomolecule or biological molecule is a loosely used term for molecules and ions that are present in organisms, essential to some typically biological process such as cell division, morphogenesis, or development.[1] Biomolecules include large macromolecules (or polyanions) such as proteins, carbohydrates, lipids, and nucleic acids, as well as small molecules such as primary metabolites, secondary metabolites, and natural products. A more general name for this class of material is biological materials. Biomolecules are usually endogenous but may also be exogenous. For example, pharmaceutical drugs may be natural products or semisynthetic (biopharmaceuticals) or they may be totally synthetic. Biology
Biology
and its subsets of biochemistry and molecular biology study biomolecules and their reactions. Most biomolecules are organic compounds, and just four elements—oxygen, carbon, hydrogen, and nitrogen—make up 96% of the human body's mass
[...More...]

"Biomolecule" on:
Wikipedia
Google
Yahoo

picture info

Protein
Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɪnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues
[...More...]

"Protein" on:
Wikipedia
Google
Yahoo

Journal Of Chromatography A
The Journal of Chromatography
Chromatography
A is a peer-reviewed scientific journal publishing research papers in analytical chemistry, with a focus on techniques and methods used for the separation and identification of mixtures. Indexed by ISI J. Chromatogr. A received an impact factor of 4.169 as reported in the 2014 Journal Citation Reports by Thomson Reuters, ranking it 15th out of 79 journals in the category “Biochemical Research Methods”[1] and ranking it sixth out of 74 journals in the category “Chemistry, analytical”.[2] See also[edit]Journal of Chromatography
Chromatography
BReferences[edit]^ "Journals Ranked by Impact: Biochemical Research Methods". 2014 Journal Citation Reports. Web of Science
Web of Science
(Sciences ed.). Thomson Reuters. 2015.  ^ "Journals Ranked by Impact: Chemistry, analytical". 2014 Journal Citation Reports
[...More...]

"Journal Of Chromatography A" on:
Wikipedia
Google
Yahoo

Distribution Constant
The distribution constant (or partition ratio) (KD), is the equilibrium constant for the distribution of an analyte in two immiscible solvents.[1][2][3] In chromatography, for a particular solvent, it is equal to the ratio of its molar concentration in the stationary phase to its molar concentration in the mobile phase, also approximating the ratio of the solubility of the solvent in each phase. The term is often confused with partition coefficient or distribution coefficient. Expression[edit] The ratio of activities of a solute, A in an aqueous/organic system will remain constant and independent of the total quantity of A (hence [ A ] o r g ∝ [ A ] a q displaystyle [A]_ org propto [A]_ aq ), so at any given temperature: ( K D )
[...More...]

"Distribution Constant" on:
Wikipedia
Google
Yahoo
.