نتایج جستجو برای: sodium dodecyl sulfate
تعداد نتایج: 229195 فیلتر نتایج به سال:
A two-step purification of pneumococcal eclipse complex is described, which uses sucrose gradient sedimentation followed by agarose gel permeation chromatography. Purified complex contains, in addition to donor DNA single strands, macromolecular material that can be labeled with methionine or leucine during development of competence. This material co-chromatographed with eclipse complex DNA on ...
Two agro-based anionic surfactants containing an isosorbide moiety have been synthesized and their amphiphilic properties evaluated. Since isosorbide is now considered as an important platform chemical of the starch industry, these compounds could represent bio-sourced alternatives to the alkyl ether sulfates (notably lauryl ether sulfate, LES) that are based on petroleum-derived ethylene oxide...
The dissociation of the extracellular hemoglobin of the earthworm Lumbricus terrestris was investigated. At neutral pH, its sz00,~ = 58.9 f 0.2 S and D:o,w = 1.61 f 0.05 X 1O-7 cm2 s-l corresponded to a molecular weight of 3.23 f 0.18 x 106. A minimum molecular weight of 24,000 per heme group was determined from the iron and heme contents, 0.221 f 0.011 weight % and 2.78 =k 0.14 weight %, respe...
The Ascaris suum intestinal basement membrane was solubilized on reduction with P-mercaptoethanol in 1% sodium dodecyl sulfate and 1% sodium dodecyl sulfate, 8 M urea to the extent of 90% and lOO%, respectively. The reduced membrane consists of at least 17 polypeptides ranging in molecular weight from 22,500 to greater than 400,000, as determined by sodium dodecyl sulfate-polyacrylamide gel ele...
A number of polyacrylamide gel systems and solubilization procedures were studied to define the number and nature of "major" polypeptide bands in the outer membrane of Pseudomonas aeruginosa. It was shown that five of the eight major outer membrane proteins were "heat modifiable" in that their mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was determined by the solubiliza...
Epoxide hydrase was solubilized from liver microsomes of phenobarbital-treated rats by treatment with cholate and purified to apparent homogeneity by ammonium sulfate fractionation and column chromatography in the presence of the nonionic detergent Emulgen 911 on DEAE-cellulose and hydroxylapatite. The purified enzyme preparation had a single major band with a molecular weight of 53,000 to 54,0...
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