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  • 1
    Electronic Resource
    Electronic Resource
    Comparative Studies on the Carbohydrate-containing membrane components of normal and virus-transformed mouse fibroblasts. II. Separation of glycoproteins and glycopeptides by Sephadex chromatography (1969)
    s.l. : American Chemical Society
    Biochemistry 8 (1969), S. 2518-2524 
    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/bi00834a039
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  • 2
    Electronic Resource
    Electronic Resource
    Carbohydrate-containing membrane components of normal and virus-transformed mouse fibroblasts. I. Glucosamine-labeling patterns in 3T3, spontaneously transformed 3T3, and SV-40-transformed 3T3 cells (1969)
    s.l. : American Chemical Society
    Biochemistry 8 (1969), S. 2509-2517 
    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/bi00834a038
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation of a purified preparation of metabolically active retinal blood vessels (1974)
    [s.l.] : Nature Publishing Group
    Nature 251 (1974), S. 65-67 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 a, Phase contrast photomicrograph of isolated bovine retinal vessel aggregate. Red blood cells are visible within vessel lumina. x 158. b, Photomicrograph of epoxy-embedded isolated bovine retinal vessel aggregate. Vessels are cut in various planes of section. Non-yascular surrounding ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/251065a0
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  • 4
    Electronic Resource
    Electronic Resource
    Small Proteins Affect Na+ Gradient-Dependent d-Glucose Transport in Isolated Renal Brush-Border Membrane Vesicles (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 456 (1985), 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.1749-6632.1985.tb14850.x
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  • 5
    Electronic Resource
    Electronic Resource
    Binding and degradation of125I-insulin by isolated rat renal brush border membranes: Evidence for low affinity, high capacity insulin recognition sites (1988)
    Springer
    The journal of membrane biology 105 (1988), S. 113-129 
    Details
    ISSN: 1432-1424
    Keywords: insulin ; brush border membranes ; kidney ; receptors ; binding ; degradation ; tubules ; protein reabsorption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The kidney plays a major role in the handling of circulating insulin in the blood, primarily via reuptake of filtered insulin at the luminal brush border membrane.125I-insulin associated with rat renal brush border membrane vesicles (BBV) in a time-and temperature-dependent manner accompanied by degradation of the hormone to trichloroacetic acid (TCA)-soluble fragments. Both association and degradation of125I-insulin were linearly proportional to membrane protein concentration with virtually all of the degradative activity being membrane assoicated. Insulin, proinsulin and desoctapeptide insulin all inhibited the association and degradation of125I-insulin by BBV, but these processes were not appreciably afected by the insulin-like growth factors IGF-I and IGF-II or by cytochromec and lysozyme, low molecular weight, filterable, proteins, which are known to be reabsorbed in the renal tubules by luminal endocytosis. When the interaction of125I-insulin with BBV was studied at various medium osmolarities (300–1100 mosm) to alter intravesicular space, association of the ligand with the vesicles was unaffected, but degradation of the ligand by the vesicles decreased progressively with increasing medium osmolarity. Therefore, association of125I-insulin to BBV represented binding of the ligand to the membrane surface and not uptake of the hormone or its degradation products into the vesicles. Attempts to crosslink125I-insulin to a high-affinity insulin receptor using the bifunctional reagent disuccinimidyl suberate revealed only trace amounts of an125I-insulin-receptor complex in brush border membrane vesicles in contrast to intact renal tubules where this complex was readily observed. Both binding and degradation of125I-insulin by brush border membranes did not reach saturation even at concentrations of insulin approaching 10−5 m. These results indicate the presence of low-affinity, high-capacity binding sites for125I-insulin on renal brush border membranes which can clearly distinguish insulin from the insulin-like growth factors and other low molecular weight proteins and polypeptides, but which do not differentiate insulin from its analogues ad do the biological receptors for the hormone. The properties and location of these binding sites make them attractive candidates for the sites at which insulin is reabsorbed in the renal tubule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02009165
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  • 6
    Electronic Resource
    Electronic Resource
    Dodecylmaltoside-Mediated Nasal and Ocular Absorption of Lyspro-Insulin: Independence of Surfactant Action from Multimer Dissociation (1998)
    Springer
    Pharmaceutical research 15 (1998), S. 1637-1639 
    Details
    ISSN: 1573-904X
    Keywords: drug delivery ; diabetes mellitus ; excipient ; insulin ; eye ; nose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1011975721569
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  • 7
    Electronic Resource
    Electronic Resource
    Ultrastructural analyses of control and enzyme-treated isolated renal basement membranes (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 200 (1981), S. 421-436 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Glomeruli and tubules were isolated from rabbit kidney cortex by mild homogenization and sieving. Mixtures of these renal components were treated with detergents to prepare pellets of morphologically intact and easily distinguishable tubular (TBM) and glomerular basement membranes (GBM). These BMs were prepared for electron microscopy after: (1) no treatment; (2) treatment with buffer alone; or (3) treatment with enzyme (pronase, trypsin, pepsin, collagenase or testicular hyaluronidase). Mixtures of TBMs and GBMs were treated in the same incubation medium to keep constant the enzyme concentration, temperature, pH, and duration of the treatment. Untreated TBMs showed collapsed, highly folded sheets of electron-dense material. In contrast, control GBMs were thinner and strikingly resistant to changes in in vivo histoarchitecture. In all enzymatic treatments except hyaluronidase, TBM was more susceptible to digestion than GBM. In general, the effect of pepsin was greater than trypsin, which was greater than pronase. Collagenase also solubilized TBM but was only slightly effective in attacking GBM. Hyaluronidase-treated BMs were indistinguishable from controls. TBMs and GBMs were both affected least by the enzyme on their epithelial surfaces, which generally remained crisp and sharply demarcated. In contrast, fibrillar materials and BM fragments were released from connective tissue surfaces of TBMs and endothelial-mesangial surfaces of GBMs. Data in the present study indicate that various BMs are morphologically heterogeneous and that a “non-unitary” concept of BM is most appropriate. Moreover, the BM “sidedness” demonstrated following enzymatic digestions strongly suggests that macromolecular complexes within laminae densae may be arranged such a manner that opposing surfaces of the same BM are compositionally disparate.
    Additional Material: 26 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092000405
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  • 8
    Electronic Resource
    Electronic Resource
    Sulfate transport in human lung fibroblasts (IMR-90) (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 125 (1985), S. 243-250 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Sulfate transport in a fibroblast cell line derived from human lung (IMR-90) occurred mainly via high- and low-affinity, SITS-sensitive pathways and to a lesser extent by an SITS-insensitive mechanism. In low-ionic-strength media (sucrose substituted for salts) the apparent Km of the carrier-mediated sulfate influx was 1 mM. At 0.3 mM, the sulfate concentration normally found in human serum, the contribution of the SITS-insensitive pathway was negligible. In physiological salts solution, an SITS-sensitive, high-affinity (Km 34 ± 14 μM) sulfate influx system was observed at extracellular sulfate concentrations less than 100 μM. Between 100 and 500 μM sulfate, the range normally found in human serum, sulfate influx occurred via an SITS-insitive, lowaffinity pathway and to a small extent by an SITS-insensitive mechanism. Extracellular chloride inhibited the influx and stimulated the efflux of sulfate. Bicarbonate and thiosulfate inhibited sulfate influx but had no effect on sulfate efflux. Phosphate, arsenate, or Na+ did not affect sulfate uptake. These results indicate that in human lung fibroblast IMR-90 cells sulfate is transported mainly via an SO42-/Cl- exchange system independent of the phosphate or Na+ transport. Since sulfate concentration as high as 50 mM only slightly increased sulfate efflux, SO42-/SO42- exchange is probably a minor component of sulfate uptake.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041250211
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