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  • Chemistry  (7)
  • Electronic structure and strongly correlated systems
  • 2010-2014
  • 1995-1999  (7)
  • 1965-1969
  • 1997  (7)
  • 1
    Electronic Resource
    Electronic Resource
    Production and characterization of a plant α-hydroxynitrile lyase in Escherichia coli (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 53 (1997), S. 332-338 
    Details
    ISSN: 0006-3592
    Keywords: α-hydroxynitrile lyase ; cassava ; cyanogenesis ; cyanohydrin ; Escherichia coli expression vector ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The coding sequence of the cyanogenic α-hydroxynitrile lyase gene of Manihot esculenta Crantz (cassava) was cloned in the plasmid vector pMal-c2 and expressed in Escherichia coli strain JM105. DNA sequencing showed that the recombinant plasmid contained the same sequence as the cDNA clone pHNL10. Peptide sequencing of the recombinant protein showed that the N-terminus was heterogeneous, with either four or six additional amino acid residues compared with the native protein. Circular dichroism spectra indicated similar secondary structure contents for both proteins. Enzyme assays showed that specific activity of native and recombinant proteins were 0.24 and 0.26 mmol CN-/mg/min, respectively; that both proteins had optimal activity at 40°C and pH 5.5; and that both proteins were inhibited by the serine protease inhibitor phenyl-methane sulfonyl flouride (PMSF). Isoelectric focusing of native and recombinant protein revealed multiple isoforms for both proteins; the recombinant protein had a more basic mean isoelectric point (pl) (5.1) than the native protein (4.5). © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 332-338, 1997.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Protein-nucleic acid interactions and DNA conformation in a complex of human immunodeficiency virus type 1 reverse transcriptase with a double-stranded DNA template-primer (1997)
    New York : Wiley-Blackwell
    Biopolymers 44 (1997), S. 125-138 
    Details
    ISSN: 0006-3525
    Keywords: AIDS ; DNA structure ; polymerase structure ; protein - DNA interaction ; x-ray crystallography ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of the DNA and the interactions of the nucleic acid with the protein in a complex of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and a 19-mer/18-mer double-stranded DNA template-primer (dsDNA) are described. The structure of this HIV-1 RT complex with dsDNA serves as a useful paradigm for studying aspects of nucleotide polymerases such as catalysis, fidelity, drug inhibition, and drug resistance. The bound dsDNA has a bend of approximately 41° at the junction of an A-form region (first five base pairs near the polymerase active site) and a B-form region (the last nine base pairs toward the RNase H active site). The 41° bend occurs smoothly over the four base pairs between the A-form portion and the B-form portion in the vicinity of helices αH and αI of the p66 thumb subdomain. The interactions between the dsDNA and protein primarily involve the sugar - phosphate backbone of the nucleic acid and structural elements of the palm, thumb, and RNase H of p66, and are not sequence specific. Amino acid residues from the polymerase active site region, including amino acid residues of the conserved Tyr-Met-Asp-Asp (YMDD) motif and the “primer grip,” interact with 3′-terminal nucleotides of the primer strand and are involved in positioning the primer terminal nucleotide and its 3′-OH group at the polymerase active site. Amino acid residues of the “template grip” have close contacts with the template strand and aid in positioning the template strand near the polymerase active site. Helix αH of the p66 thumb is partly inserted into the minor groove of the dsDNA and helix αI is directly adjacent to the backbone of the template strand. Amino acid residues of Β1′, αA′, αB′, and the loop containing His539 of the RNase H domain interact with the primer strand of the dsDNA. © 1997 John Wiley & Sons, Inc. Biopoly 44: 125-138, 1997
    Additional Material: 8 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    Chromate Conversion Coatings on 2024 Al Alloy (1997)
    Chichester [u.a.] : Wiley-Blackwell
    Surface and Interface Analysis 25 (1997), S. 223-234 
    Details
    ISSN: 0142-2421
    Keywords: conversion coating ; aluminium ; alloy ; x-ray photoelectron spectroscopy ; scanning electron microscopy ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: X-ray photoelectron spectroscopy (XPS), scanning electron microscopy (SEM) and potentiodynamic measurements have been made on chromate conversion-coated Al 2024-T3 alloy. X-ray photoelectron spectroscopy measurements indicated that the conversion coating had a surface of CrOOH and Cr(VI), enriched in ferricyanide. The bulk of the coating was an equal mixture of CrOOH and Cr2O3 with significant levels of F- and Fe, the latter implying the presence of ferricyanide throughout the coating. Copper(II) ion was present at the interface between the conversion coating and the alloy, as well as Al3+. During ageing experiments, potentiodynamic measurements indicated that the corrosion current (icorr) decreased from ∽0.4 to ∽0.04 μA cm-2 during the first 40 h after preparation but thereafter slowly increased. No significant changes were observed in the chemistry of the coating by XPS for ageing times longer than 40 h, although morphological changes were observed with SEM. As the coating aged, a network of microcracks developed across the surface. It is believed that Cr6+ is consumed in the process in which plugs of hydrated chromium oxide form at the base of these cracks. © 1997 by John Wiley & Sons, Ltd.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Standardized characterization of gene expression in human colorectal epithelium by two-dimensional electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2842-2848 
    Details
    ISSN: 0173-0835
    Keywords: Colonic neoplasms ; Rectal neoplasms ; Two-dimensional polyacrylamide gel electrophoresis ; Cell separation ; Antibodies' monoclonal diagnostic use ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: New diagnostic and prognostic markers are needed in colorectal cancer. They can be found by differential analysis at DNA, RNA or protein level. The accuracy of phenotypic comparisons of tumor and normal tissues depends on the purity of the samples. We present an effective method to identify and isolate proteins that are differentially expressed under altered conditions, and a two-dimensional reference protein map of the normal human colonic epithelium Normal colonic mucosa, primary tumors and liver metastases were prepared in the operating room. After washing in an ice-cold medium containing protease inhibitors, crypts were isolated by mechanical preparation without using metalloproteinases. Epithelial cells were then selected using Ber-EP4 Dynabeads. The samples were denaturated before processing for immobilized pH gradient two-dimensional polyacrylamide gel electrophoresis according to SWISS-2DPAGE standards. The samples contained more than 95% epithelial cells as confirmed by fluorescence-activated cell sorting using pan-anticytokeratin antibodies. Cell surfaces were not damaged, as assessed by scanning electronic microscope. A protein reference map of the normal colonic epithelium was defined. Using gel matching, N-terminal sequencing and/or immunoblotting techniques, 60 polypeptides - including proteins specifically expressed in colorectal epithelium - have now been identified. This reproducible method of sample preparation permits the comparison of protein patterns found in various pathological states with the present reference map (http://www.expasy.ch). Some of these patterns might provide diagnostic or prognostic markers, or even molecular targets for therapy in the future.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181520
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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Renal cell carcinoma and normal kidney protein expression (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 599-604 
    Details
    ISSN: 0173-0835
    Keywords: Kidney ; Two-dimensional polyacrylamide gel electrophoresis ; Renal cell carcinoma ; Database ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Renal cell carcinoma (RCC), a human kidney cancer from the proximal tubular epithelium, accounts for about 3% of adult malignancies. Molecular and cytogenetic analysis have highlighted deletions, translocations, or loss of heterozygosity in the 3p21-p26, a putative RCC locus, as well as in 6q, 8p, 9pq, and 14pq. Studies on phenotypic expression of human kidney tissue and on post-translational modifications in RCC have not yet provided a marker for early renal cell carcinoma diagnosis. Current dignostic methods do not help to detect the tumor before advanced stages. We therefore used two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) to study normal and tumor kidney tissues in ten patients suffering from RCC. A human kidney protein map in the SWISS-2DPAGE database accessible through the ExPASy WWW Molecular Biology Server was established. Of 2789 separated polypeptides, 43 were identified by gel comparison, amino acid analysis, N-terminal sequencing, and/or immunodetection. The comparison between normal and tumor kidney tissues showed four polypeptides to be absent in RCC. One of them was identified as ubiquinol cytochrome c reductase (UQCR), whose locus has elsewhere been tentatively assigned to chromosome 19p12 or chromosome 22. A second polypeptide was identified as mitochondrial NADH-ubiquinone oxido reductase complex I whose locus is located on chromosome 18p 11.2 and chromosome 19q 13.3. These result suggest that the lack of UQCR and of mitochondrial NADH-ubiquinone oxidoreductase complex I expression in RCC may be caused by unknown deletions, or by changes in gene transcription or translation. It might indicate that mitochondrial disfunction plays a major role in RCC genesis or evolution.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180343
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