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  • 1
    Digitale Medien
    Digitale Medien
    Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator (1980)
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 4653-4659 
    Details
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/bi00561a018
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  • 2
    Digitale Medien
    Digitale Medien
    Mouse 7S nerve growth factor: complete sequence of a cDNA coding for the .alpha.-subunit precursor and its relationship to serine proteases (1984)
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 5997-6002 
    Details
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/bi00320a015
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  • 3
    Digitale Medien
    Digitale Medien
    Lectin from sainfoin (Onobrychis viciaefolia Scop.). Complete amino acid sequence (1984)
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 1824-1830 
    Details
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/bi00303a038
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  • 4
    Digitale Medien
    Digitale Medien
    Sciatin Is a Transferrin-Like Polypeptide (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: Sciatin, an acidic glycoprotein from chicken sciatic nerve, has myotrophic effects on avian skeletal muscle cells in culture. As sciatin was found to have certain structural similarities to transferrin, we further investigated the physicochemical characteristics of sciatin in order to determine the relationship between these two proteins. Sciatin was found to be strikingly similar to ovotransferrin in amino acid composition. In addition, amino acid sequence analysis revealed that sciatin and ovotransferrin had identical amino-terminal sequences for at least the first 20 amino acid residues. Chicken ovotransferrin, but not human serum transferrin, cross-reacted with rabbit antisciatin antibodies upon rocket immunoelectrophoresis and double immunodiffusion in agar. In addition, in the presence of bicarbonate, sciatin bound approximately 2 mol ferrous iron/mol protein. Using the purification procedure developed for sciatin, we purified a protein from chicken serum that cross-reacted with antisciatin serum, migrated at a position identical to that of sciatin or ovotransferrin on two-dimensional gel electrophoresis, had an amino composition very similar to ovotransferrin and sciatin, and had myotrophic effects on cultured muscle cells. From these data, we conclude that sciatin is a growth-promoting polypeptide closely related in structure to transferrin.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb03949.x
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  • 5
    Digitale Medien
    Digitale Medien
    Neurobiology: What cloned genes can tell us about nerve growth factor (1983)
    [s.l.] : Nature Publishing Group
    Nature 303 (1983), S. 751-751 
    Details
    ISSN: 1476-4687
    Quelle: Nature Archives 1869 - 2009
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Notizen: [Auszug] IN the more than three decades since its discovery!, nerve growth factor (NGF) has proved to be an uncommonly valuable source of insight into the developmental biology of the peripheral nervous system in particular2, and growth regulatory molecules in general. It has provided an im portant ...
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1038/303751a0
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  • 6
    Digitale Medien
    Digitale Medien
    Histidine residue modification inhibits binding of murine β nerve growth factor to its receptor (1984)
    Springer
    The protein journal 3 (1984), S. 349-356 
    Details
    ISSN: 1573-4943
    Schlagwort(e): diethylpyrocarbonate ; protein conformation ; synthetic peptide ; insulin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract The reaction of the β subunit of murine nerve growth factor (NGF) with diethylpyrocarbonate (DEP) results in the quantitative modification of histidine residues and the loss of binding to rabbit superior cervical ganglia microsomes. No conformational changes accompanied the conversion as judged by fluorescence spectra. Hydroxylamine converted the carbethoxy derivatives back to the unmodified imidazoles and simultaneously restored the capacity of NGF to bind to its receptor. Modification of des (1–9) NGF, from which His-4 and His-8 have been quantitatively removed, results in the same loss in binding activity, suggesting that His-75 and/or His-84 may play an important role in hormone-receptor interactions.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025171
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  • 7
    Digitale Medien
    Digitale Medien
    Purification and partial characterization of bovine pituitary fibroblast growth factor (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 195-208 
    Details
    ISSN: 0730-2312
    Schlagwort(e): pituitary fibroblast growth factor ; silver staining ; amino acid analysis ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods [3,4] which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of ∼20-fold, was achieved by electro-phoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500-15,00 as determined on SDS gels, chromatographs as a monomer in nondenaturing conditions, and is active at the picomolar level in effecting the incorporation of 3H-thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jcb.240210302
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  • 8
    Digitale Medien
    Digitale Medien
    Polypeptide growth factors: Some structural and mechanistic considerations (1980)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 14 (1980), S. 183-199 
    Details
    ISSN: 0091-7419
    Schlagwort(e): primary and secondary hormones ; mitogenicity ; insulin ; insulin-like growth factor ; nerve growth factor ; relaxin ; epidermal growth factor ; receptor-mediated endocytosis ; lysomes ; hormone mechanisms ; Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Polypeptide growth factors are substances that stimulate an increase in cell size and/or cell number during embryonic development. In some cases, they have a similar effect on tissues in the mature organism where they function as “maintenance” factors to sustain cell viability. While their profound impact on cell behavior is well recognized, their relationship to other regulators of cell function has remained generally ill-defined. However, the developing appreciation of their hormone-like behavior suggests that they may be conveniently grouped with many other endocrine agents to form a broader group of secondary hormones. The utility of the classification is illustrated by the insulin-related family of molecules. It also serves to emphasize the similarities in function shared by many of these substances including trophic stimulation and modulation of gene expression. Internalization, though, appears to be another common feature. However, whether the uptake of the growth factor mediates an intracellular action or is designed solely to regulate responsiveness at the cell surface and/or degradation remains an important unanswered question. A brief review of two growth factors (nerve growth factor and epidermal growth factor) serves to outline the possible functions that may be served by this endocytotic process.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jss.400140207
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