Modification of Seaweed Polysaccharide-agarose and Its Application as Skin Dressing——Degradation of Agarose and Its Features
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Abstract The adsorption kinetics of myoglobin in charged gels of varying agarose content have been measured macroscopically, through batch uptake experiments, and microscopically, using light microscopy with gels supported in microfluidics chips. The apparent effective pore diffusivities, determined by fitting either set of rate data to the shrinking core model, were greater than the free solution diffusivity and concentration‐dependent. Moreover, the microscopically derived concentration profiles were qualitatively different from the predicted ones. Therefore, a new model taking into account an assumed favorable partitioning of the protein in the pore liquid is proposed to describe the adsorption kinetics. The new model yields effective pore diffusivities that are in approximate agreement with the values determined chromatographically under nonbinding conditions and with hindered diffusion theory. In addition, it predicts concentration profiles in the gel that are consistent with those observed microscopically. The overall increase in mass transfer is attributed to the favorable partitioning of the protein in the pores at low ionic strength, which results in a greater diffusional driving force. © 2008 American Institute of Chemical Engineers AIChE J, 2009
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This paper discusses the effects of gel composition and separation temperature on the migration properties of fluorescein-5-isothiocyanate-labeled protein molecular mass markers (ranging from 20 100 to 205 000 Da) in automated ultrathin-layer sodium dodecyl sulfate (SDS) gel electrophoresis. The separation mechanism with the agarose and composite agarose - linear polyacrylamide, agarose - hydroxyethyl cellulose, and agarose - polyethylene oxide matrices were all found to comply with the Ogston sieving model in the molecular mass range of the protein molecules investigated. Our temperature studies revealed that electrophoretic separation of SDS protein complexes is an activated process and, in pure agarose and in composite agarose - hydroxyethyl cellulose and agarose - polyethylene oxide matrices that the separation requires increasing activation energy as a function of the molecular mass of the separated proteins. On the other hand, when linear polyacrylamide was used as composite additive, the activation energy demand of the separation decreased with increasing solute molecular mass. The sensitivity of the laser-induced fluorescent detection of the automated ultrathin-layer electrophoresis system was evaluated by injecting a series of dilutions of the markers and was found to be less than 2.5 ng/band for the fluorophore-labeled protein.
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Sodium dodecyl sulfate
Molecular-weight size marker
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Polyacrylamide
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Methods for separating proteins according to molecular weight are usually based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). However, the toxicity of acrylamide and its handling during gel preparation constitute a significant problem. Therefore, we determined the molecular weights of proteins using agarose gel instead of polyacrylamide. We used the Mupid electrophoretic apparatus, because it is small, easy to use, and time-saving. We evaluated different types of agarose and buffer solutions, and parameters such as gel concentration, buffer SDS concentration, and quantity of gel (central thickness). The optimal gel was made from 5ml (central gel thickness 2mm) 4% NuSieve 3:1 agarose. An electrophoresis buffer containing 25mM Tris, 190mM glycine (pH8.3), and 0.1% SDS is optimal for protein separation. With this method, the standard curve was linear for reference proteins in the range of molecular weights from 14.4×103 to 97×103.
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Sodium dodecyl sulfate
Molecular-weight size marker
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By using agarose as the raw material,agarose spheres are prepared based on the reverse suspension principle.The particle sizes of those spheres range from 45μm to 165μm.The obtained agarose spheres can be further cross-linked for enhanced mechanical strength,which can be further derivatized with carboxymethyl agents.The effects of reagent amount,the reaction temperature and time are performed to maximize ion exchange capacity.The final carboxymethyl containing agarose spheres are used for the separation and purification of crude alkaline protease and show comparable efficiency with the similar foreign products.
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Abstract A simple procedure for the preparation of agarose suitable for electrophoresis is developed in which anionic polysaccharides are removed by extracting the agar gel-granules with phosphate buffer (0.03 M, pH 6.8)containing urea (4 M), followed by electrophoresis in the same buffer system. Further, alkali treatment in the presence of sodium borohydride, eliminates electroendosmosis, giving essentially a neutral agarose, as Judged by the electrophoretic behaviour of basic substances like crystal violet and cytochrome C. The purified agarose with yields 60–65%, has a sulphur content less than 0.1%, and forms rigid, transparent gels.
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A preparative method for isolating centigram quantities of high molecular weight polypeptide chains with high resolution and recovery uses linear polyacrylamide/agarose composite (LPAC) gels as electrophoretic media from which the polypeptides can be easily extracted. The composites are prepared in a manner yielding linear copolymers of acrylamide and 1-allyloxy-2,3-propanediol within 2% agarose gels. After electrophoresis in sodium dodecyl sulfate (SDS), protein bands were rapidly visualized for excision by briefly immersing the gel in cold 0.1 M KCl which precipitates the protein-associated SDS. The gel slices are then freeze-thawed to disrupt the agarose matrix and promote syneresis of fluid upon centrifugation. The polypeptides are then separated from the polyacrylamide in the supernatant solution by precipitating with either acidic isopropanol, trichloroacetic acid, ammonium sulfate or other general protein precipitants. As determined with polypeptide chains of fibrinogen and its cross-linked derivatives, recoveries were virtually complete (95.4% +/- 2.2%), and were independent of molecular weights over the range tested (10(4) --10(6)).
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Abstract The electrophoretic separation of RNA species in composite ultra low/medium gelling temperature agarose is described. The resolution obtained was superior to that observed with the standard medium gelling temperature agarose alone. Poly(A)‐containing mRNA was successfully fractionated and recovered in a biologically active form from the separating media.
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