sodium-dodecyl-sulfate and Carcinoma--Ehrlich-Tumor

sodium-dodecyl-sulfate has been researched along with Carcinoma--Ehrlich-Tumor* in 9 studies

Other Studies

9 other study(ies) available for sodium-dodecyl-sulfate and Carcinoma--Ehrlich-Tumor

ArticleYear
A multifunctional protein: involvement of the alpha-1 serum protease inhibitor in SDS and high salt-stable DNA-protein complexes.
    FEBS letters, 1997, Aug-11, Volume: 413, Issue:1

    Occasionally new and intriguing roles arise for proteins with well established functions. The alpha-1 serum protease inhibitor (alpha-1 PI) represents another example. Sequence identities exist in the alpha-1 PI and in a nuclear 52-kDa glycoprotein which is involved in resistant DNA-polypeptide complexes. The results of Western blots support the identity of the two proteins and immunocytochemical studies indicate the nuclear location of the alpha-1 PI. Consistently, e.g. Ehrlich ascites tumor cells express the alpha-1 PI, and the fusion protein between the alpha-1 PI and the green fluorescent protein from Aequorea victoria shows intracellular accumulation and partly nuclear location.

    Topics: alpha 1-Antitrypsin; Amino Acid Sequence; Animals; Blotting, Western; Carcinoma, Ehrlich Tumor; DNA-Binding Proteins; Endopeptidase K; Fluorescent Antibody Technique, Indirect; Molecular Sequence Data; Recombinant Proteins; Sodium Dodecyl Sulfate

1997
High salt- and SDS-stable DNA binding protein complexes with ATPase and protein kinase activity retained in chromatin-depleted nuclei.
    Nucleic acids research, 1995, Apr-25, Volume: 23, Issue:8

    Cell lysis in presence of SDS and proteinase K followed by salting-out of residual polypeptides by dehydration and precipitation with saturated sodium chloride solution [Miller, S.A., Dykes, D.D. and Polesky, H.F., Nucleic Acids Res., 16, 1215, 1988] efficiently resolves deproteinized DNA. However, this DNA is still associated with prominent polypeptides which remain stably attached to DNA during further treatments, e.g. during repeated salting-out steps, prolonged incubation of DNA in 1% SDS or 4 M urea at 56 degrees C and ethanol precipitation. The persistent polypeptides (62, 52 and 40 kDa) released from Ehrlich ascites cell DNA were further characterized. Microsequencing indicates that the DNA binding polypeptides are not yet characterized at the sequence level. Nuclease digestion of the DNA releases stable DNA-protein complexes with the shape of globular particles (12.8 +/- 0.8 nm) and their larger aggregates in which DNA remains protected from nuclease digestion. The isolated DNA-polypeptide complexes show ATPase (Km = 7.4 x 10(-4) M) and protein kinase activity. Antibodies reveal a parallel distribution of the complexes with chromatin, however, the complexes are retained in chromatin-depleted nuclei.

    Topics: Adenosine Triphosphatases; Amino Acid Sequence; Animals; Carcinoma, Ehrlich Tumor; Cell Nucleus; DNA; DNA-Binding Proteins; Immunologic Techniques; Molecular Sequence Data; Molecular Weight; Protein Kinases; Sodium Chloride; Sodium Dodecyl Sulfate; Species Specificity

1995
Effect of lysolecithin and analogs on mouse ascites tumors.
    Cancer research, 1978, Volume: 38, Issue:2

    Topics: Animals; Carcinoma, Ehrlich Tumor; Dose-Response Relationship, Drug; Female; Fibrosarcoma; Lysophosphatidylcholines; Male; Mice; Mice, Inbred Strains; Neoplasm Transplantation; Sarcoma, Experimental; Sodium Dodecyl Sulfate; Surface-Active Agents; Time Factors

1978
Cell-free translation of immunoglobulin messenger RNA from MOPC-315 plasmacytoma and MOPC-315 NR, a variant synthesizing only light chain.
    Proceedings of the National Academy of Sciences of the United States of America, 1975, Volume: 72, Issue:1

    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 tested programmed the synthesis of the heavy chain in this system. Analysis of cell-free products by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by immunoprecipitation demonstrated that no translatable heavy chain mRNA could be extracted from the MOPC-315 NR variant plasmacytoma.

    Topics: Animals; Carcinoma, Ehrlich Tumor; Cell-Free System; Electrophoresis, Polyacrylamide Gel; Immunoglobulin A; Immunoglobulin Fragments; Immunoglobulin Heavy Chains; Immunoglobulins; Methionine; Mice; Myeloma Proteins; Neoplasms, Experimental; Plasmacytoma; Precipitin Tests; Protein Biosynthesis; RNA, Messenger; RNA, Neoplasm; Sodium Dodecyl Sulfate; Sulfur Radioisotopes

1975
Biological activity of 125iodine labelled globin mRNA in an Ehrlich ascites cell-free system.
    Molecular biology reports, 1974, Volume: 1, Issue:6

    Topics: Animals; Birds; Carcinoma, Ehrlich Tumor; Cell-Free System; Centrifugation, Density Gradient; Chromatography, DEAE-Cellulose; Chromatography, Gel; Erythrocytes; Globins; Iodine Radioisotopes; Leucine; Protein Biosynthesis; Ribonucleases; RNA, Messenger; Sodium Dodecyl Sulfate; Spectrophotometry, Ultraviolet; Tritium

1974
Early ribonuclease scissions and the stucture of ribosomes.
    Biochimica et biophysica acta, 1974, May-17, Volume: 349, Issue:2

    Topics: Animals; Carcinoma, Ehrlich Tumor; Cell Line; Centrifugation, Density Gradient; Cricetinae; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Guinea Pigs; Kidney; Kinetics; Liver; Molecular Weight; Pancreas; Ribonucleases; Ribonucleotides; Ribosomes; RNA, Bacterial; RNA, Ribosomal; Sodium Dodecyl Sulfate; Species Specificity; Time Factors; Ultracentrifugation; Urea

1974
Studies on the hetrogeneity of lysine-rich histones in dividing cells.
    The Journal of biological chemistry, 1974, Jun-25, Volume: 249, Issue:12

    Topics: Amino Acids; Animals; Ascitic Fluid; Carcinoma, Ehrlich Tumor; Cattle; Cell Division; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Histones; Lactones; Liver; Lysine; Mice; Molecular Weight; Organ Specificity; Peptide Fragments; Rats; Sodium Dodecyl Sulfate; Species Specificity; Spiro Compounds; Succinimides; Thymus Gland; Trypsin

1974
The ribosome cycle in mammalian protein synthesis. II. Association of the native smaller ribosomal subunit with protein factors.
    The Journal of biological chemistry, 1973, Jun-25, Volume: 248, Issue:12

    Topics: Adenine; Animals; Carbon Isotopes; Carcinoma, Ehrlich Tumor; Cell Line; Centrifugation, Density Gradient; Culture Media; Cytoplasm; Densitometry; Electrophoresis, Polyacrylamide Gel; Formates; Kinetics; Molecular Weight; Neoplasm Proteins; Peptide Initiation Factors; Protein Binding; Ribosomes; RNA, Neoplasm; RNA, Ribosomal; Sodium Dodecyl Sulfate; Spectrophotometry, Ultraviolet; Tritium

1973
Properties of nascent DNA of Ehrlich ascites tumor cells obtained by nitrocellulose column chromatography.
    Biochemical and biophysical research communications, 1972, Oct-06, Volume: 49, Issue:1

    Topics: Animals; Carbon Isotopes; Carcinoma, Ehrlich Tumor; Cellulose; Centrifugation, Density Gradient; Chromatography; DNA, Neoplasm; DNA, Single-Stranded; Hydroxyapatites; Male; Methods; Mice; Mice, Inbred Strains; Nitro Compounds; Nucleic Acid Conformation; Peptide Chain Initiation, Translational; Sodium Dodecyl Sulfate; Tritium; Uridine

1972
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