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  • 1
    Electronic Resource
    Electronic Resource
    Identification and subcellular localization of a 21-kilodalton molecule using affinity-purified antibodies against .alpha.-transforming growth factor (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 2067-2070 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00381a041
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  • 2
    Electronic Resource
    Electronic Resource
    FLUORESCENTLY-LABELED CALMODULIN LOCALIZES SPECIFIC SITES ON MITOCHONDRIA (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 356 (1980), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1980.tb29643.x
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  • 3
    Electronic Resource
    Electronic Resource
    Immunological detection and quantitation of alpha transforming growth factors in human breast carcinoma cells (1986)
    Springer
    Breast cancer research and treatment 7 (1986), S. 201-210 
    Details
    ISSN: 1573-7217
    Keywords: αTGFs ; breast cancer cells ; estrogen ; estrogen receptor ; p21ras protein ; radioimmunoassay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Alpha transforming growth factors (αTGFs) were immunologically detected in the concentrated conditioned medium (CM) prepared from four human breast cancer cell lines and from primary cultures of human mammary epithelial cells, and in the tissue extracts prepared from normal, benign, and malignant breast biopsies. Immunoreactive αTGFs were quantitated by a competitive radioimmunoassay (RIA) using affinity-purified polyclonal sheep anti-rat αTGF antibodies which react with human αTGF but not with human epidermal growth factor (EGF). The relative level of RIA-detectable αTGFs in the CM from the breast cancer cell lines MCF-7, ZR-75-1, T47-D, and MDA-MB-231, and from the CM of primary cultures of human mammary epithelial cells, ranged from 0.02 to 0.85 ng/ml. MCF-7 or ZR-75-1 cells grown in the presence of 17β-estradiol (10−8 M) for 48 h were found to release two- to three-fold more αTGFs into their CM than the same cells grown in the absence of estrogen. In detergent extracts prepared from normal breast tissue, a benign fibrocystic lesion, fibroadenomas and primary breast carcinomas, the relative αTGF concentrations were found to range from 1.5 to 6 ng/mg cell protein. No significant correlations were found between the αTGF levels and the pathological state of the tissues, the estrogen receptor status of the tumors, or the relative amounts of theras gene protein p21ras in the tissues as determined by Western immunoblot analysis. The question of biological relevancy of αTGF for human mammary tumors will require further studies on (a) synthesis and turnover of αTGF, (b) the relationship between immunoreactivity and biological activity of αTGF, and (c) differences in biological responsiveness of mammary tumor cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01806251
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  • 4
    Electronic Resource
    Electronic Resource
    Human A673 cells secrete high molecular weight EGF-receptor binding growth factors that appear to be immunologically unrelated to EGF or TGF-α (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 32 (1986), S. 247-259 
    Details
    ISSN: 0730-2312
    Keywords: epidermal growth factor ; transforming growth factors ; NRK colony formation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Extracts of serum-free conditioned medium from human rhabdomyosarcoma A673 cells contain high molecular weight (HMW) transforming growth factors (TGFs) that can be partially purified by Bio-Gel P-100 and carboxymethyl (CM)-cellulose chromatography (Todaro et al: Proc Natl Acad Sci USA 77:5258, 1980). Reversephase high performance liquid chromatography (HPLC) revealed a principal peak of epidermal growth factor (EGF) radioreceptor assay (RRA) activity and anchorage-independent growth (AIG) activity that coeluted with 25-26% acetonitrile. If a trailing shoulder of EGF RRA activity from the CM-C chromatography was included in the material for HPLC analysis, additional active fractions were observed at 21-22% acetonitrile. Importantly, both active regions from HPLC failed to compete in radioimmunoassays under reduced and denatured conditions for human EGF (hEGF), human TGF-α- (hTGF-α), or rat TGF-α (rTGF-α) and failed to give positive signals in Western blots under conditions in which TGF-α was readily detected when using an antisera raised against the 17 C-terminal amino acids of rTGF-α. Nonreducing sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed EGF RRA and AIG activities in gel slices corresponding to Mr 15,000 and 22,000 in the 25-26% acetonitrile eluate and Mr 15,000, 20,000, 27,000, and 48,000 in the 21-22% acetonitrile eluate. The presence of multiple forms of EGF-receptor-binding peptides produced in vitro suggest size heterogeneity and possible immunologic diversity among high molecular weight members of the EGF/TGF-α family of growth-promoting polypeptides.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240320402
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