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Dextran is a complex branched glucan (polysaccharide derived from the condensation of glucose), originally derived from wine. IUPAC defines dextrans as "Branched poly-α-d-glucosides of microbial origin having glycosidic bonds predominantly C-1 → C-6". [ 1 ]
The collected fractions are often examined by spectroscopic techniques to determine the concentration of the particles eluted. Common spectroscopy detection techniques are refractive index (RI) and ultraviolet (UV). When eluting spectroscopically similar species (such as during biological purification), other techniques may be necessary to ...
Sephadex is a cross-linked dextran gel used for gel filtration. It was launched by Pharmacia in 1959, after development work by Jerker Porath and Per Flodin. [1] [2] The name is derived from separation Pharmacia dextran. It is normally manufactured in a bead form and most commonly used for gel filtration columns. By varying the degree of cross ...
Dextran 1 is composed of a small fraction (1 kilodalton) of the entire dextran complex. This is enough to bind anti-dextran antibodies but insufficient to result in the formation of immune complexes and resultant immune responses. Thereby, dextran 1 binds up antibodies towards dextran without causing the immune response, leaving less antibodies ...
[1] [2] Fractions are collected based on differences in a specific property of the individual components. A common trait in fractionations is the need to find an optimum between the amount of fractions collected and the desired purity in each fraction. Fractionation makes it possible to isolate more than two components in a mixture in a single run.
Dextran and oxidized dextran can be used to crosslink gelatin microspheres to reduce gelatin dissolution, which slows the drug release rate. These dextran/gelatin microspheres can be used to provide slow-release of TRAPP-Br, which is a cancer therapeutic. [ 8 ]
Lysate proteins are eluted along an ionic strength gradient and fractions are collected over short time intervals. Each fraction is analyzed by LC-MS/MS for both protein and drug content. Individual proteins elute with characteristic profiles, and pre-incubated drugs should mirror the elution profiles of the targets they complex with.
The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [2] spectroscopic analytical procedure used to measure the concentration of protein in a solution.