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  • Molecular Cell Biology  (7)
  • Wiley-Blackwell  (7)
  • 1985-1989
  • 1980-1984  (7)
  • 1940-1944
  • 1981  (7)
  • 1942
  • 1
    Electronic Resource
    Electronic Resource
    The transforming sequences of avian myelocytomatosis virus (MC29) (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 16 (1981), S. 193-207 
    Details
    ISSN: 0275-3723
    Keywords: recombinant DNA ; acute leukemia virus ; bacleriophage λ ; R-looping ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Avian myelocytomatosis virus (MC29), a defective acute leukemia virus, has a broad oncogenic spectrum in vivo, and transforms fibroblasts and hematopoietic target cells in vitro. We have used recombinant DNA technology to isolate and characterize the sequences that are essential in the transformation process. Integrated MC29 proviral DNA was isolated from a library of recombinant phage containing DNA from the MC29-transformed nonproducer quail cell line Q5. The cloned DNA was analyzed by Southern blotting of restriction endonuclease digests and by electron microscopic visualization of R-loops formed between the cloned DNA and MC29 or helper virus RNA. It was found that the 9.2 kb cloned DNA insert contains approximately 4 kb of viral sequences and 5.2 kb of quail cellular sequences. The viral sequences contain all of the MC29-specific sequences and 5′ helper related sequences as well as part of the envelope region. The size of the cloned EcoRI fragment is the same as that of the major band in EcoRI-cleaved Q5 DNA that hybridizes to viral sequences. Transfection of the cloned DNA into NIH 3T3 cells revealed that the MC29-specific sequences are functional in that they induce foci of trans-formed cells with high efficiency.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380160209
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  • 2
    Electronic Resource
    Electronic Resource
    Cleavage of cell surface proteins by thrombin (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 15 (1981), S. 49-61 
    Details
    ISSN: 0275-3723
    Keywords: labeling of cell surface proteins ; two-dimensional gel electrophoresis ; fibronectin ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: This study was based on our previous findings that the mitogenic action of thrombin on cultured fibroblasts can result from interaction of thrombin with the cell surface in the absence of internalization, and that the proteolytic activity of thrombin is required for stimulation of cell division. This prompted us to look for thrombin-mediated cleavages using 2-dimensional gel electrophoresis of labeled cell surface proteins. Surface membrane components were labeled by 3 procedures: (1) proteins were labeled by lactoperoxidase-catalyzed iodination using 125I-; (2) galactose and galactosamine residues of glycoproteins were oxidized with galactose oxidase and reduced with 3H-NaBH4; and (3) glycoproteins were metabolically labeled by incubating cells with 3H-fucose. Labeling with the first 2 procedures was carried out after thrombin treatment; in contrast, cells metabolically labeled with 3H-fucose were subsequently treated with thrombin to look for proteolytic cleavages. Collectively, these studies indicated that only about 5 cell surface proteins were thrombin-sensitive, consistent with the high specificity of this protease. Each of the labeling procedures revealed a thrombin-sensitive cell surface glycoprotein which was identified as fibronectin by immunoprecipitation experiments. In addition, cell surface proteins of about 140K and 55K daltons were thrombin-sensitive. However, cell surface proteins of about 45K daltons and 130K to 1 50K daltons were increased after thrombin treatment. These experiments were conducted on an established line of Chinese hamster lung cells with the eventual goal of studying thrombin-mediated cleavages of cell surface proteins in a large number of cloned populations derived from this line that are either responsive or unresponsive to the mitogenic action of thrombin. This approach should permit identification of proteolytic cleavages that are necessary for thrombin-stimulated cell division.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380150106
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  • 3
    Electronic Resource
    Electronic Resource
    Murine teratocarcinoma: A model for virus-cell interaction in a differentiating cell system (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 15 (1981), S. 205-211 
    Details
    ISSN: 0275-3723
    Keywords: murine teratocarcinoma ; embryonal carcinoma ; SV40 ; infection ; T antigen ; immunoprecipitation ; replication ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The stem cell of the murine teratocarcinoma is refractory to infection with Simian virus 40 and polyoma. Utilizing various procedures, we attempted to alter this block to infection by modifying the infection procedure. Multiple infections with high-titer SV40 and pretreatment of cells with DEAE-dextran or the carcinogen 4-nitroquinoline l-oxide did not induce embryonal carcinoma cells to produce T- antigen. Co-infection with adenovirus 5, which infects the embryonal carcinoma, and SV40 did not induce the expression of SV40 Tantigen. Therefore, these procedures did not overcome the block to virus infection. The assay for the SV40 T antigen was immunofluorescence; however, the immunoprecipitation technique did not detect T antigen in the infected embryonal carcinoma cells. Finally, the viral DNA present in the embryonal carcinoma was examined for its ability to replicate. These studies showed that viral DNA was not replicating as assayed by the viral DNA's sensitivity to UV irradiation when replicating in the presence of 5-bromodeoxyundine.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380150211
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  • 4
    Electronic Resource
    Electronic Resource
    Phosphoproteins in dictyostelium discoideum (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 15 (1981), S. 369-385 
    Details
    ISSN: 0275-3723
    Keywords: membrane phosphoproteins ; cAMP in development ; Dictyostelium discoideum ; phospho proteins ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The phosphoproteins of Dictyostelium discoideum were compared at different stages of development by polyacrylamide gel electrophoresis. Certain phosphoproteins of vegetative amoebae were conserved while others appeared and disappeared during development. Four major phosphoproteins with apparent subunit molecular weights of 50,000, 47,000, 38,000, and 34,000 disappeared precociously in response to exogenous cAMP. Two membranal phosphoproteins, with apparent subunit molecular weights of 80,000 and 81,000, appeared precociously in response to added cAMP. One of these phosphoproteins, molecular weight of 80,000, has been identified tentatively as the “contact site A” glycoprotein. Another membranal protein, with apparent subunit molecular weight of 42,000, unaffected in its appearance by cAMP, has been identified tentatively as phosphoactin.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380150407
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  • 5
    Electronic Resource
    Electronic Resource
    Monoclonal antibody covalently coupled to liposomes: Specific targeting to cells (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 16 (1981), S. 243-258 
    Details
    ISSN: 0275-3723
    Keywords: liposomes ; liposome-protein coupling ; fluorescence ; monoclonal antibody ; cell surface antigens ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have evaluated optimal conditions for coupling monoclonal antibody to small unilamellar lipisomes. Coupling of an IgG2a monoclonal anti-β2-microglobulin antibody, which reacts with human cells, was examined in detail. Liposomes were composed of dipalmitoyl lecithin and cholesterol, and variable quantities of phosphatidylethanolamine substituted with the heterobifunctional cross-linking reagent N-hydroxysuccinimidyl 3-(2-pyridyldithio) propionate (SPDP). They were reacted with antibody derivatized with the same reagent at a 5- to 20-fold molar excess, and activated by mild reduction. This degree of SPDP modification had no effect on the capacity of the antibody to bind to its target antigen. More than 40% of antibody could be reproducibly bound to liposomes, resulting in the coupling of from 1 to 10 antibody molecules per liposome (mean diameter.580 Å). The coupling reaction did not lead to loss of carboxyfluorescein encapsulated within liposomes. At least 80% of liposomes carried nondenatured antibody, as confirmed by precipitation of liposomes and encapsulated carboxyfluorescein by Staphylococcus aureus, strain Cowan I. The liposome-coupled antibody retained its immunological specificity: only cells expressing human β2-microglobulin bound liposomes in vitro, and the binding was inhibited by the free antibody in solution. Results with antibodies of different antigenic specificity confirm that the technique can be generally applied.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380160305
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  • 6
    Electronic Resource
    Electronic Resource
    Immunological analysis of a glycoprotein (contact sites A) involved in intercellular adhesion of dictyostelium discoideum (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 197-211 
    Details
    ISSN: 0275-3723
    Keywords: adhesion ; Dictyostelium discoideum ; contact sites A ; development ; immune staining after polyacrylamide gel electrophoresis ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have prepared antisera in rabbits to the “contact sites A” glycoprotein (gp80) purified from Dictyostelium discoideum. IgG isolated from these anti-sera reacts with a number of different proteins in D discoideum lysates, as analyzed by immune precipitation and by antibody staining of gel electropherograms transferred to nitrocellulose. Blocking experiments indicate that this cross-reactivity reflects the presence of common antigeneic determinants on gp80 and other cellular proteins, rather than the presence of extraneous antibodies in the antisera. The spectrum of reactive proteins is different a: different stages of development. In particular, gp80 itself is synthesized only for a restricted period during the cell aggregation phase. The protein persists throughout development and can be detected in spores. Anti-gp80 Fab fragments bind to the surface of developing D discoideum cells and specifically block their developmentally regulated adhesion. After absorption with vegetative cells, the IgG stains only gp80 and (to a lesser extent) one other band in lysates of aggregation-competent cells. The absorbed antibodies also can block adhesion. Several proteins that appear late in development also arc stained by the absorbed IgG.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.380170302
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  • 7
    Electronic Resource
    Electronic Resource
    The resolution of two populations of lysosomal organelles containing endocytosed wistaria floribunda agglutinin from murine fibroblasts (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 337-346 
    Details
    ISSN: 0275-3723
    Keywords: endocytosis ; GERL ; lectin ; lysosome ; subcellular fractionation ; Wistaria floribunda ; agglutinin ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Subcellular fractionation of Balb/c 3T3 fibroblasts exposed to Wistaria floribunda agglutinin was performed to localize fractions containing internalized lectin. Employing two sequential self-generating silica sol density gradients, the postnuclear supernatant of cell homogenates was resolved into five distinct cellular components. Lysosome enzyme activities were displayed by two populations of vesicles, each separated from plasma membrane, golgi, and mitochondria markers. The more dense of these fractions exhibited morphological and biochemical properties ascribed to secondary lysosomes: The more buoyant population was similar to that reported by Rome et al [11] who noted that it may be a product of vesiculated golgi endoplasmic reticulum lysosome (GERL). Treatment with W floribunda agglutinin of cells, surface radioiodinated demonstrated that plasma membrane proteins were localized within both the buoyant and dense lysosome populations in as little as 10 min after exposure to lectin. Prolonged incubation of the cells with W floribunda agglutinin resulted in maintenance of this distribution. However, when nonradiactive cells were exposed to 125I-labeled W floribunda agglutinin for 10 min, radioactivity was detected only in the buoyant population of lysosomes as well as the plasma membrane/golgi fraction. Treatment of cells with W floribunda agglutinin for 30 min resulted in appearance of lectin associated radioactivity in the dense lysosome fraction in addition to those populations containing radioactivity seen after a 10-min incubation. These data indicate that the endocytosis of W floribunda agglutinin differed substantially from the internalization of a portion of the plasma membrane proteins. Furthermore, we found radioactivity associated with both plasma membrane proteins W floribunda agglutinin in regions of the density gradient fractionation that virtually lacked golgi and lysosome markers. These fractions may have represented populations of nonlysosome vesicles formed during the process of endocytosis.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.380170405
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