نتایج جستجو برای: sodium dodecyl sulfate polyacrylamide

تعداد نتایج: 240620  

Journal: :Cancer research 1973
N Kadohama R W Turkington

The acidic chromatin proteins extracted from normal and neoplastic mammary cells of C3H mice and Fischer rats have been compared by polyacrylamide gel electrophoresis, amino acid analysis, and radioactivity labeling patterns of synthesis in vitro. Following purification of chromatin from purified nuclei and extraction of histones in 2 M sodium chloride, the acidic proteins associated with DNA w...

Journal: :Journal of bacteriology 1976
D W Yem H C Wu

beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophenyl-beta-D-2-acetamido-2-deoxyglucopyranoside is 0.43 mM. The molecular weight of this enzyme, determined by bo...

Journal: :The Journal of biological chemistry 1972
A M Weiner T Platt K Weber

A simple, rapid, manual technique is described for determining the amino-terminal amino acid sequence of proteins on a nanomole scale. In this modification of the 5-dimethylaminonaphthalene-1-sulfonyl-Edman degradation, inorganic carriers permit convenient manipulation of small amounts of protein, and use of the detergent sodium dodecyl sulfate throughout the procedure maintains protein solubil...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1975
M Green P N Graves T Zehavi-Willner J McInnes S Pestka

Total poly(A)-containing mRNA was isolated from the MOPC-315 and MOPC-315 NR plasmacytomas. The RNA was further fractionated on sodium dodecyl sulfate-sucrose gradients. The MOPC-315 mRNA fractions directed the synthesis of both the heavy chain and light chain precursor of the MOPC-315 IgA protein in a cell-free extract of Ehrlich ascites tumor cells. None of the MOPC-315 NR mRNA fractions test...

Journal: :The Journal of biological chemistry 1980
G N Levy D Aminoff

Exo-alpha-N-acetylgalactosaminidase has been purified 8000-fold from Clostridium perfringens by gel filtration, ion exchange chromatography, isoelectric precipitation, and negative adsorption on human O type erythrocytes. The resulting enzyme is active at physiological pH and temperature. Phenyl glycosides, oligosaccharides, mucins, glycolipids, and cell membranes are substrates for this enzyme...

Journal: :Journal of virology 1972
D J Bucher E D Kilbourne

Neuraminidase activity of influenza virus was directly seen on sodium dodecyl sulfate polyacrylamide gels with the aid of the synthetic substrate, methoxyphenol neuraminic acid. Neuraminidase (NA) appeared as a high-molecular-weight fraction with a size in the range of 220,000 to 250,000 daltons. Isolation of this fraction from the X-7 strain of influenza virus, dissociation with sodium dodecyl...

2002
ULRICH K. LAEMMLI

A rapid and convenient method for peptide mapping of proteins has been developed. The technique, which is especially suitable for analysis of proteins that have been isolated from gels containing sodium dodecyl sulfate, involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis. The pattern of pept...

A. R. Alborzi, M. R. Seyfiabad Shapouri N. Hoghooghi Rad

Exsheathing fluid (EF) and excretory-secretory products (ES) of infective third-stage cultured larvae ofOstertagia circumcincta were analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDSPAGE). Five and seven predominant proteins were found in the EF and ES products, respectively. Immunoblotting by sheep pre-infection serum did not react with any of the EF and ES proteins, b...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1988
T A Brown J M Prahl H F DeLuca

Monoclonal antibodies against the porcine 1,25-dihydroxyvitamin D3 receptor were immobilized on Sepharose CL-4B and used to obtain a highly purified 1,25-dihydroxyvitamin D3 receptor fraction with a 45% recovery of the 1,25-dihydroxyvitamin D3 binding capacity. The porcine receptor was purified to homogeneity by preparative electrophoresis and digested in sodium dodecyl sulfate/polyacrylamide g...

Journal: :Antimicrobial agents and chemotherapy 1977
E Katz H Felix

Vaccinia virus antigens, in HeLa cells treated with the antipox virus drug isatin beta-thiosemicarbazone (IBT), were analyzed by immunoprecipitation, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The total radioactivity in the immunoprecipitate was decreased to almost 50% in the presence of the drug as compared to its absence. An inhibition also occurred with an IBT-dep...

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