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  • 1
    Electronic Resource
    Electronic Resource
    A two-dimensional protein map of human amniotic fluid at 17 weeks' gestation (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2816-2822 
    Details
    ISSN: 0173-0835
    Keywords: Amniotic fluid ; Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradient ; Protein map ; Gel matching ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Using updated technical procedures (immobilized pH gradients for isoelectric focusing followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis: IPG/SDS-PAGE) we provide a two-dimensional (2-D) map of amniotic fluid (AF) proteins. This map comprises over 800 silver-stained spots. Over 150 spots have been identified by matching on the net with human plasma and cerebrospinal fluid maps available from SWISS 2DPAGE database; several additional spots were assigned by immunoblotting and/or microanalytical techniques. This report details our investigation on AF proteins focusing on the 17th week of gestation, when AF is most commonly used for clinical evaluation of fetal disorders. As a whole, the map displays a number of potential markers for fetal development and for gestation abnormalities. The 2-D electrophoretic technique allows the monitoring of all these proteins at the same time along with additional spots that may prove of diagnostic significance.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181517
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Charge heterogeneity of macrophage migration inhibitory factor (MIF) in human liver and breast tissue (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2010-2013 
    Details
    ISSN: 0173-0835
    Keywords: Breast biopsy ; Two-dimensional polyacrylamide gel electrophoresis ; Macrophage migration inhibitory factor ; Liver biopsy ; Breast cell line ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Macrophage migration inhibitory factor (MIF) is an ubiquitous protein playing various immunological and hormonal roles. Theoretical electrophoretic coordinates calculated from protein sequence in the SWISS-PROT database (AC P14174) are 12 kDa and pI 8.24. Using two-dimensional (2-D) immunoblotting, we have detected isoelectric forms at ca. 11.9 kDa, with pI values of 7.8 and 6.98 in human liver tissue, breast tissue and a cell line and in preparations of human MIF expressed in E. coli. This evidence suggests that MIF charge heterogeneity originates from a post-translational modification not requiring euka-ryote-specific enzymes. We have also detected in human liver a minor immunoreactive spot at pI 6.23, which coincides with the MIF spot in the liver map in SWISS-2DPAGE. The pI 6.23 isoform also conceivably derives from post-translational modification, as MIF is known to be encoded in the human genome by a single copy gene.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191120
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoretic patterns of acute-phase human serum proteins in the course of bacterial and viral diseases (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 612-616 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional electrophoresis ; Serum proteins ; Acute phase ; Infectious diseases ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Acute-phase serum proteins were analyzed by two-dimensional electrophoresis with isoelectric focusing in 3-10 immobilized pH gradients. Most spots were identified by reference to the plasma map in the SWISS-2DPAGE database. Serum amyloid A protein spots were identified by immunoblotting with specific antiserum and by matching determined with predicted values of electrophoretic parameters. Changes in the concentrations of α1-antitrypsin, leucinerich glycoprotein, haptoglobin, serum retinol-binding protein and transthyretin were quantitated by densitometry of silver-stained gels. Electrophoretic patterns from 18 patients with bacterial diseases and 16 patients with viral diseases were compared. The incidence of serum amyloid A protein spots was 18/18 in bacterial diseases and 6/16 in viral diseases. As for the other reactants studied, variations were simultaneous in bacterial disease and tended to be staggered in viral diseases.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170333
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  • 4
    Electronic Resource
    Electronic Resource
    Acute-phase proteins in perinatal human plasma (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 520-526 
    Details
    ISSN: 0173-0835
    Keywords: Acute-phase serum ; Neonate ; Haptoglobin ; Serum amyloid A protein ; Two-dimensional polyacrylamide gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Plasma from eight newborns (4 pre-term and 4 full-term) with early-onset (〈72 h) sepsis and six apparently healthy controls was analyzed. The presence of spots identified as haptoglobin and serum amyloid A protein was the electrophoretic result most consistently associated with disease. Time course monitoring showed rises, peaks and declines of spot intensity as expected for acute-phase proteins induced by transient stimuli. Haptoglobin β chains appear to be undersialated in pre-term newborns, whereas post-translational modifications of α chains and serum amyloid A protein are similar to those observed in adults. The undersialation of β chain and occurrence of α chain phenotypes different from those found in maternal serum indicate that perinatal haptoglobin originates from neonatal synthesis.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180331
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    Paper (German National Licenses)
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