نتایج جستجو برای: sds polyacrylamide gel electrophoresis
تعداد نتایج: 131538 فیلتر نتایج به سال:
conclusions our successful extraction of purified lps from e. coli isolates of uti patients’ urine samples can be an important step to understand the uti disease conditions. results the silver-stained gel demonstrated both smooth and rough type lps by showing trail-like band patterns with the presence and lacking o-antigen region, respectively. coomassie blue staining showed no band assuring th...
the domesticated silkworm, bombyx mori linn., a lepidopteran molecular model and an important economic insect that are emerging as an ideal molecular genetic resource for solving a broad range of biological problems. the silkworm, b. mori produces massive amount of silk proteins during the final stage of larval development. these proteins are stored in the middle silk gland and they are dischar...
Probably the most widely used of techniques for analyzing mixtures of proteins is SDS polyacrylamide gel electrophoresis. In this technique, proteins are reacted with the anionic detergent, sodium dodecylsulfate (SDS, or sodium lauryl sulfate) to form negatively charged complexes. The amount of SDS bound by a protein, and so the charge on the complex, is roughly proportional to its size. Common...
background and objectives: making stacking gels for polyacrylamide gels in the laboratory by conventional methods is laborious and time consuming. considering the role of temperature in polyacrylamide gels with respect to electrical resistance and viscosity, we assumed that decreasing the temperature would cause an increase in electrical resistance and viscosity. ultimately, a downward tempera...
(1983) Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods in Enzymology 91: 227. Laas T (1989) Electrophoresis in gels. In: Janson J-C and Ryden L (eds) Protein PuriTcation } Principles, High Resolution Methods and Applications. New York, Weinheim and Cambridge: VCH Publishers. Laemmli UK (1970) Cleavage of structural proteins during...
The final purification of the three-fraction enzyme complex mycobacillin synthetase was done by hydroxyapatite column chromatography and sucrose-density-gradient centrifugation; each of the fractions obtained migrates as a single component in SDS/polyacrylamide-gel electrophoresis and gel electrofocusing. The Mr of the enzyme fractions A, B and C by gel filtration is 260 000, 190 000 and 105 00...
Renin was purified from 47 kg of hog kidney to produce enough enzyme for enzymatic and physicochemical characterization. The procedure included extraction at pH 3.5 in the presence of protease inhibitors, two ammonium sulfate precipitations, ion exchange chromatography on Sepharose-hexamethylenediamino-pepstatin gel, gel filtration, and isoelectric focusing. Renin, 2.3 mg, with a specific activ...
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