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  • 1
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Fetal and neonatal rats were treated with dexamethasone in vivo and the effect of this treatment on the 35kDa surfactant-associated protein was examined. Dexamethasone treatment increased the levels of translatable mRNA for the 35kDa protein from day 19 of gestation until at least 6 days after birth. Prior to gestational day 19, no glucocorticoid effect was seen although the mRNA was detectable as early as gestational day 16. Similar results were seen when [35S]methionine-labeled 35kDa protein was immunoprecipitated and subjected to two-dimensional gel electrophoresis.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Glucocorticoids are known to enhance fetal lung maturation. Previous studies with whole lung have shown that specific proteins are enhanced by these hormones. At least two effects of glucocorticoids on fetal lung epithelia require the presence of mesenchymal elements. Since the lung consists of several different cell types, further understanding of glucocorticoid effects on fetal lung protein synthesis requires that such studies be carried out with specific cell types. Using two-dimensional gel electrophoresis, we have examined the synthesis and secretion of proteins by fetal rat lung fibroblasts in the presence and absence of glucocorticoid. Two proteins, fsa and fsb, are enhanced by dexamethasone, appear to be organ specific, and are enhanced only during prenatal and early postnatal life. They are not enhanced by a variety of other hormones.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 231-233 
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Studies from several laboratories involving amino acid analysis and sequencing of the Mr 35 000 pulmonary surfactant-associated proteins (SP-A) have detected hydroxyproline residues. These residues are present in a region with a collagen-like sequence that has been revealed by direct amino acid sequencing and from the deduced amino acid sequence of the cDNA clones coding for SP-A. We treated human lung tissue with tunicamycin to block N-glycosylation and with 2,2-dipyridyl to inhibit the hydroxylation of proline residues. The SP-A synthesized under these conditions showed a shift in apparent molecular weight to 27 000 and 29 000 compared to 29 000 and 31 000 for SP-A synthesized in the presence of tunicamycin alone. Dipyridyl treatment alone caused an alteration in electrophoretic mobility similar to that seen with tunicamycin, although this was more difficult to evaluate since changes in molecular weight due to glycosylation occurred under these conditions. These results indicate that proline hydroxylation in the collagen-like portion of SP-A decreases its electrophoretic mobility.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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