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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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  • 2
    Electronic Resource
    Electronic Resource
    Protein expression profiles in human breast ductal carcinoma and histologically normal tissue (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2832-2841 
    Details
    ISSN: 0173-0835
    Keywords: Ductal breast carcinoma ; Breast biopsy ; Two-dimensional polyacrylamide gel electrophoresis ; Reference map ; Immobilized pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Reference two-dimensional (2-D) gels are presented for human breast ductal carcinoma and histologically normal tissue. Whole biopsy fragments were analyzed, including epithelial and nonepithelial components. Thirty-five spots have been assigned by gel matching to the human liver SWISS-2DPAGE reference map and/or to the human primary keratinocyte IPG map from the Danish Center for Human Genome. N-terminal microsequencing was applied to confirm randomly chosen matching assignments and to identify six new spots. Protein expression profiles in ductal carcinoma and in normal breast tissue appeared to be similar, except for a pattern consisting of 32 spots, which were highly expressed in all carcinoma specimens, and less intense and occasionally undetectable in normal tissue. This difference was statistically significant. Assignment has been obtained for several spots, namely GRP94, GRP78, GRP75, mitochondrial HSP60, calreticulin, protein disulfide isomerase, peptidyl-prolyl cis-trans isomerase, collagen-binding protein 2, fructose bisphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, thioredoxin, cytochrome c oxidase VA subunit, tubulin β isoform and macrophage migration inhibitory factor (MIF). The cancer- and tissue-specificity of the described pattern was assessed by matching to the Swiss-2DPAGE human liver, hepatoma, lymphoma, erythroleukemia reference maps. The pattern of 32 spots was found to be indicative of epithelial neoplasia.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181519
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  • 3
    Electronic Resource
    Electronic Resource
    Mapping of Chlamydia trachomatis proteins by Immobiline-polyacrylamide two-dimensional electrophoresis: Spot identification by N-terminal sequencing and immunoblotting (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 185-190 
    Details
    ISSN: 0173-0835
    Keywords: Chlamydia ; Two-dimensional polyacrylamide gel electrophoresis ; Protein maps ; Immobilized pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Proteins from purified elementary bodies of Chlamydia trachomatis were separated by two-dimensional gel electrophoresis on nonlinear wide-range immobilized pH gradients in the first dimension and polyacrylamide gradient gels in the second dimension. The maps obtained with this system are highly reproducible and resolve ca. 600 spots. By using immunoblot analysis with specific antibodies and/or N-terminal amino acid sequencing, we established the positions of a number of described chlamydial proteins, such as the major outer membrane protein (MOMP) the 60 kDa cystein-rich outer membrane protein (OMP2), the DnaK-like, GroEL-like, and macrophage infectivity potentiator (MIP)-like proteins, the plasmid-encoded pgp3 protein, two ribosomal proteins (S1 and L7/L12), and the protein-elongation factor EF-Tu. Other proteins, for which gene assignment was not possible, have been identified by three parameters (Mr, pI and N-terminal sequence). This work provides a preliminary basis for a future and progressive compilation of a genome-linked database of chlamydial proteins.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170130
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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Two-dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 851-853 
    Details
    ISSN: 0173-0835
    Keywords: Human albumin ; Penicillin ; Two-dimensional polyacryl-amide gel electrophoresis ; Immunoblotting ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A two-dimensional gel electrophoresis and immunoblotting procedure has been developed to assess the level of modification by penicillins in human serum albumin. The procedure can be used in in vitro experiments and in clinical studies with sera from patients treated with penicillins.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601140
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  • 6
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1190-1192 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Immunoblotting ; Serum proteins ; Ampicillin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional electrophoretograms of serum proteins from ampicillintreated patients were analyzed by immunoblotting with an antiserum specific for penicilloyl groups. As expected, human serum albumin (HSA) was the main ampicilloylated serum component. Transferrin main form II was found to be the second most important component as regards immunoblotting intensity. Immunoreactive spots were present on the acidic side of the transferrin isoelectric series, suggesting a modification mechanism similar to that observed in HSA, i.e., acylation of basic amino acid residues. Several additional ampicilloylated spots were detected but could not be assigned. Their electrophoretic parameters were determined using internal standards. This is the first description of serum proteins other than HSA being modified by ampicillin in the course of routine therapeutic treatment.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601198
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  • 7
    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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  • 8
    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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