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  • 1
    Electronic Resource
    Electronic Resource
    Determination of micro amounts of mercury(I) iodide in mercury(II) iodide by Raman spectrometry
    Amsterdam : Elsevier
    Analytica Chimica Acta 253 (1991), S. 155-159 
    Details
    ISSN: 0003-2670
    Keywords: Mercury ; Mercury iodide ; Raman spectrometry
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0003-2670(91)87170-C
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Determination of micro amounts of mercury(I) iodide in mercury(II) iodide by Raman spectrometry
    Amsterdam : Elsevier
    Vibrational Spectroscopy 2 (1991), S. 155-159 
    Details
    ISSN: 0924-2031
    Keywords: Mercury ; Mercury iodide ; Raman spectrometry
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0924-2031(91)85021-E
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    Paper (German National Licenses)
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  • 3
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    Decorin and biglycan of normal and pathologic human corneas (1998)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: PURPOSE: Corneas with scars and certain chronic pathologic conditions contain highly sulfated dermatan sulfate, but little is known of the core proteins that carry these atypical glycosaminoglycans. In this study the proteoglycan proteins attached to dermatan sulfate in normal and pathologic human corneas were examined to identify primary genes involved in the pathobiology of corneal scarring. METHODS: Proteoglycans from human corneas with chronic edema, bullous keratopathy, and keratoconus and from normal corneas were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), quantitative immunoblotting, and immunohistology with peptide antibodies to decorin and biglycan. RESULTS: Proteoglycans from pathologic corneas exhibit increased size heterogeneity and binding of the cationic dye alcian blue compared with those in normal corneas. Decorin and biglycan extracted from normal and diseased corneas exhibited similar molecular size distribution patterns. In approximately half of the pathologic corneas, the level of biglycan was elevated an average of seven times above normal, and decorin was elevated approximately three times above normal. The increases were associated with highly charged molecular forms of decorin and biglycan, indicating modification of the proteins with dermatan sulfate chains of increased sulfation. Immunostaining of corneal sections showed an abnormal stromal localization of biglycan in pathologic corneas. CONCLUSIONS: The increased dermatan sulfate associated with chronic corneal pathologic conditions results from stromal accumulation of decorin and particularly of biglycan in the affected corneas. These proteins bear dermatan sulfate chains with increased sulfation compared with normal stromal proteoglycans.
    Keywords: Life Sciences (General)
    Type: Investigative ophthalmology & visual science (ISSN 0146-0404); 39; 10; 1957-64
    Format: text
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    NASA TECHNICAL REPORTS
  • 4
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    Fibroblast growth factor-2 promotes keratan sulfate proteoglycan expression by keratocytes in vitro (2000)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: Keratocytes of the corneal stroma produce a specialized extracellular matrix responsible for corneal transparency. Corneal keratan sulfate proteoglycans (KSPG) are unique products of keratocytes that are down-regulated in corneal wounds and in vitro. This study used cultures of primary bovine keratocytes to define factors affecting KSPG expression in vitro. KSPG metabolically labeled with [(35)S]sulfate decreased during the initial 2-4 days of culture in quiescent cultures with low serum concentrations (0.1%). Addition of fetal bovine serum, fibroblast growth factor-2 (FGF-2), transforming growth factor beta, or platelet derived growth factor all stimulated cell division, but only FGF-2 stimulated KSPG secretion. Combined with serum, FGF-2 also prevented serum-induced KSPG down-regulation. KSPG secretion was lost during serial subculture with or without FGF-2. Expression of KSPG core proteins (lumican, mimecan, and keratocan) was stimulated by FGF-2, and steady state mRNA pools for these proteins, particularly keratocan, were significantly increased by FGF-2 treatment. KSPG expression therefore is supported by exogenous FGF-2 and eliminated by subculture of the cells in presence of serum. FGF-2 stimulates KSPG core protein expression primarily through an increase in mRNA pools.
    Keywords: Life Sciences (General)
    Type: The Journal of biological chemistry (ISSN 0021-9258); 275; 18; 13918-23
    Format: text
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    NASA TECHNICAL REPORTS
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