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  • Life and Medical Sciences  (5)
  • 1985-1989  (5)
  • 1985  (5)
Document type
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  • 1985-1989  (5)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Solubilization, reconstitution, and attempted affinity chromatography of the sugar transporter of the erythrocyte membrane (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 83-96 
    Details
    ISSN: 0730-2312
    Keywords: human erythrocytes ; glucose transport ; membrane transport ; reconstitution ; membrane protein solubilization ; affinity chromatography ; phloretin derivatives ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Reconstitution of the sugar transport system of human erythrocytes into artificial liposomes was achieved by freezing, thawing, and sonicating preformed phospholipid vesicles in the presence of intact ghosts, protein-depleted ghosts, or detergent-treated ghosts. D-glucose equilibrium exchange activities and affinity constants in the range of the reported erythrocyte values were reached in the best experiments. Whereas the extraction of peripheral membrane proteins did not depress the transport function crucially after reconstituting these protein-depicted ghosts, the selective Solubilization of integral membrane proteins by a variety of nonionic detergents resulted in an uncontrollable, continuously increasing inactivation of the carrier. However, Emulphogene BC-720 extracts could be prepared in which the glucose transporter retained activity for days at 4°C. These extracts were applied to affinity chromatography matrices of phloretin-Agarose, prepared by coupling phloretinyl-3′-benzylamine (PBA) to CH-Sepharose 4B and to Affigel 202. Although the solubilized sugar transporter appeared to be selectively adsorbed to both PBA matrices, it could not be eluted by specific counter ligands or gentle eluants in a biologically active form. However, chaotropic agents could be used to elute intrinsic proteins, including bands 3 and 4. 5, from the Affigel affinity medium.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270203
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of the epidermal growth factor receptor by phosphorylation (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 195-208 
    Details
    ISSN: 0730-2312
    Keywords: epidermal growth factor receptor ; protein-tyrosine kinase ; self-phosphorylation ; protein kinase C ; oncogene ; growth factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The receptor for epidermal growth factor (EGF) is a glycosylated transmembrane phosphoprotein that exhibits EGF-stimulable protein tyrosine kinase activity. On EGF stimulation, the receptor undergoes a self-phosphorylation reaction at tyrosine residues located primarily in the extreme carboxyl-terminal region of the protein. Using enzymatically active EGF receptor purified by immunoaffinity chromatography from A431 human epidermoid carcinoma cells, the self-phosphorylation reaction has been characterized as a rapid, intramolecular process which is maximal at 30-37°C and exhibits a very low Km for ATP (0.2 μM). When phosphorylation of exogenous peptide substrates was measured as a function of receptor self-phosphorylation, tyrosine kinase activity was found to be enhanced two to threefold at 1-2 mol of phosphate per mol of receptor. Analysis of the dependence of the tyrosine kinase activity on ATP concentration yielded hyperbolic kinetics when plotted in double-reciprocal fashion, indicating that ATP can serve as an activator of the enzyme. Higher concentrations of peptide substrates were found to inhibit both the self- and peptide phosphorylation, but this inhibition could be overcome by first self-phosphorylating the enzyme. These results suggest that self-phosphorylation can remove a competitive/inhibitory constraint so that certain exogenous substrates can have greater access to the enzyme active site. In addition to self-phosphorylation, the EGF receptor can be phosphorylated on threonine residues by the calcium- and phospholipid-dependent protein kinase C. The sites on the EGF receptor phosphorylated in vitro by protein kinase C are identical to the sites phosphorylated on the receptor isolated from A431 cells exposed to the tumor promoters 12-O-tetradecanoylphorbol 13-acetate or teleocidin. This phosphorylation of the EGF receptor results in a suppression of its tyrosine kinase and EGF binding activities both in vivo and in vitro. The EGF receptor can thus be variably regulated by phosphorylation: self-phosphorylation can enhance tyrosine kinase activity whereas protein kinase C-catalyzed phosphorylation can depress enzyme activity. Because these two phosphorylations account for only a fraction of the phosphate present in the EGF receptor in vivo, other protein kinases can apparently phosphorylate the receptor and these may exert additional controls on EGF receptor/kinase function.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240290304
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Canalicular communication in the cortices of human long bones (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 212 (1985), S. 336-344 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A scanning electron microscopic (SEM) cast method that has been utilized to examine the internal structure of dentine was modified to examine canalicular communications in the cortices of a human femur and ulna. Although some preparations in which all of the matrix was removed were examined, etched preparations were found to be the most informative. Casts of lacunae and canaliculi along with the underlying matrix could be visualized in these preparations. In the femur, whose cortex exhibited a typical lamellar pattern, canalicular communication was seen between first and second generation osteons and occasionally between osteons and interstitial regions. The interstitial regions in the ulna appeared to be primarily woven rather than lamellar bone. Extensive communication between the outermost lacunae of osteons and interstitial regions was observed in the ulna.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092120403
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  • 4
    Electronic Resource
    Electronic Resource
    Scanning electron microscopic observations of casts of human dentinal tubules along the interface between primary and secondary dentine (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 211 (1985), S. 149-155 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A scanning electron microscope cast technique was used to examine the interface between primary and secondary dentine in young and old human teeth. In addition, more traditional methods were used to examine this interface with light microscopy, identical regions being viewed before and after demineralization. No continuity was seen between the tubules in primary dentine and those in irregular secondary dentine in the scanning electron microscope preparations. These preparations did show the tubules to be continuous between primary dentine and regular secondary dentine in young and old teeth. Both the scanning electron microscopic and light microscopic observations suggested that regular secondary dentine becomes highly sclerosed in old teeth.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092110206
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  • 5
    Electronic Resource
    Electronic Resource
    Toxic compounds: From metabolism studies to prediction. Foregin Compound Metabolism. Edited by J. CALDWELL and P. C. PAULSON. Taylor and Francis, 1984. Pp. 328. £32 (1985)
    New York, NY : Wiley-Blackwell
    BioEssays 2 (1985), S. 282-283 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950020612
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    Paper (German National Licenses)
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