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  • Two-dimensional polyacrylamide gel electrophoresis  (3)
  • kinetics  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Ring dehydration mechanisms and kinetics of polyamic acid models in solution and in the solid state (1993)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 31 (1993), S. 2839-2854 
    Details
    ISSN: 0887-624X
    Keywords: polyamic acid models ; kinetics ; mechanisms ; RMN solid-state rayons X ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We have synthesized and studied the ring dehydration mechanisms and kinetics of polyamic acid models in solution and in the solid state using 13C-NMR (solid and liquid), HPLC, FTIR, and x-ray diffraction. Results obtained in solution show the role of temperature, catalysts, and the basicity of the amine in ring dehydration mechanisms and kinetics, as well as conformation and intramolecular bonds in the amic acid bond in the solid state. © 1993 John Wiley & Sons, Inc.
    Additional Material: 25 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1993.080311122
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Mechanism of thermal polymerization of cyanate ester systems: Chromatographic and spectroscopic studies (1996)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 34 (1996), S. 2955-2966 
    Details
    ISSN: 0887-624X
    Keywords: cyanate esters ; spectroscopies ; kinetics ; catalysts ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The mechanisms and kinetics of polymerization of mono- and difunctional cyanate esters are investigated using chromatographic (HPLC) and spectroscopic methods (UV, liquid and solid-state NMR, and FTIR). The results obtained after chromatographic separation and identification of the chemical species present in the reaction medium have enabled us to propose a reaction path and a kinetic model for these thermally polymerized systems. Finally, the polymerization of cyanate ester was studied in the presence of different catalysts (imidazole, AcAcCu and AcAcCr) added directly, without solvent, and showed their influence on mechanisms. © 1996 John Wiley & Sons, Inc.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    Reactions of the double-stranded oligonucleotide d(TTGGCCAA)2 with cis-[Pt(NH3)2(H2O)2]2+ and [Pt(NH3)3(H2O)]2+Kinetic Analysis of the Reactions Between GG-Containing Oligonucleotides and Platinum Complexes, Part II. Part I: Reactions of Single-Stranded Oligonucleotides with cis-[Pt(NH3)2(H2O)2]2+ and [Pt(NH3)3(H2O)]2+, ref.[15]. (1996)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 2 (1996), S. 1068-1076 
    Details
    ISSN: 0947-6539
    Keywords: antitumor agents ; DNA ; kinetics ; platinum complexes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The kinetics of the reactions between the GG-containing double-stranded oligonucleotide d(TTGGCCAA)2 (II) and the platinum complexes cis-[Pt-(NH3)2(H2O)2]2+ (1) and [Pt(NH3)3-(H2O)]2+ (2) were studied and compared with those already determined for the reactions of the single-stranded octanucleotide d(CTGGCTCA) (I).[1] The results were as follows: i) Complex 1 reacted faster than 2 with both I and II. ii) Both complexes 1 and 2 reacted faster with II than with I. This acceleration was greater for 1 (x 13) than for 2 (x4) and only due to the increase of the platination rate of the 5′-G of the GG sequence. iii) For both I and II, the first platination by 1 and 2 was faster on the 5′-G than on the 3′-G. This difference was more significant for the platination of II (k5′/k3′ = 12 for 1 and 5 for 2) than of I (k5′/k3′ ≤ 2). iv) The cyclization reaction of the monoadducts (G*) of 1 to yield the GG cis-Pt(NH3)2+2 chelate (G*G*) was considerably slowed down in the duplex. This rate decrease was significantly larger for the chelation of the 5′-G* (factor of 16) than of the 3′-G* (factor of 4) monoadducts. v) The intrastrand chelation of the 3′-G* monoaducts (k3′c) was faster than that of the 5′-G* monoadducts (k5′c), both for I and II (k3′c/k5′c = 3 and 13, respectively). vi) In addition to the intrastrand G*G* crosslink, we also observed the interstrand crosslink d(GG*CC)-d(GG*CC) between the two 3′-Gs of the central tetranucleotide. The rate constant for the interstrand crosslinking (k3′i) was half that of the intrastrand chelation (k3′c). vii) The 5′ monoadduct, which was formed faster (k5′ 〈 k3′) and was chelated more slowly (k5′c 〉 k3′i 〈 k3′c), exhibited a half-life of 3.2 h under our experimental conditions.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chem.1460020904
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  • 4
    Electronic Resource
    Electronic Resource
    Melanie II - a third-generation software package for analysis of two-dimensional electrophoresis images: I. Features and user interface (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2724-2734 
    Details
    ISSN: 0173-0835
    Keywords: Melanie ; Computer analysis ; Two-dimensional polyacrylamide gel electrophoresis ; World Wide Web ; Federated database ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Although two-dimensional electrophoresis (2-DE) computer analysis software packages have existed ever since 2-DE technology was developed, it is only now that the hardware and software technology allows large-scale studies to be performed on low-cost personal computers or workstations, and that setting up a 2-DE computer analysis system in a small laboratory is no longer considered a luxury. After a first attempt in the seventies and early eighties to develop 2-DE analysis software systems on hardware that had poor or even no graphical capabilities, followed in the late eighties by a wave of innovative software developments that were possible thanks to new graphical interface standards such as XWindows, a third generation of 2-DE analysis software packages has now come to maturity. It can be run on a variety of low-cost, general-purpose personal computers, thus making the purchase of a 2-DE analysis system easily attainable for even the smallest laboratory that is involved in proteome research. Melanie II 2-D PAGE, developed at the University Hospital of Geneva, is such a third-generation software system for 2-DE analysis. Based on unique image processing algorithms, this user-friendly object-oriented software package runs on multiple platforms, including Unix, MS-Windows 95 and NT, and Power Macintosh. It provides efficient spot detection and quantitation, state-of-the-art image comparison, statistical data analysis facilities, and is Internet-ready. Linked to proteome databases such as those available on the World Wide Web, it represents a valuable tool for the “Virtual Lab” of the postgenome area.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181506
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  • 5
    Electronic Resource
    Electronic Resource
    Improved and simplified in-gel sample application using reswelling of dry immobilized pH gradients (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 324-327 
    Details
    ISSN: 0173-0835
    Keywords: Sample application ; Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradient ; Protein characterization ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A simple and inexpensive methacrylate rehydration chamber was built to accomodate ten immobilized pH gradient (IPG) strips. In the chamber, entire IPG gels were used for sample application, with the protein entering the gels during their rehydration. For rehydration, commercially available or laboratory-made strips were positioned in the grooves with the gel in contact with 500 μL of sample for 6 h or overnight. This avoided the use of sample cups, eliminated precipitation at the sample application site, thus improving resolution over the entire pH range of the gels. It also allowed precise control of protein amounts and sample volumes loaded into the IPG gels, and also lowered costs of reagents during rehydration and equilibration owing to the reduced volumes. Up to 5 mg of protein can be loaded on wide IPG gels and up to 15 mg of some samples on narrow pH range gels.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180305
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Translationally controlled tumor protein: A protein identified in several nontumoral cells including erythrocytes (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 150-155 
    Details
    ISSN: 0173-0835
    Keywords: Calcium-binding protein ; Two-dimensional polyacrylamide gel electrophoresis ; Growth related protein ; Post-translational modification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The translationally controlled tumor protein (TCTP) is a growth-related protein which is regulated at the translational level. It is present in mammals, higher plants and Saccharomyces cerevisiae. This study was undertaken to localize and further characterize the TCTP in human cell lysates using two-dimensional gel electrophoresis, monoclonal antibodies, and 45Ca-gel overlay. TCTP was found in several healthy and tumoral cells including erythrocytes, hepatocytes, macrophages, platelets, keratinocytes, erythroleukemia cells, gliomas, melanomas, hepatoblastomas, and lymphomas. It could not be detected in kidney and renal cell carcinoma (RCC). A monoclonal antibody raised against TCTP detected three isoforms likely due to post-translational modifications. A calcium binding property was found as well as heat stability and cytoplasmic localization. The high degree of homology from plants to man and its expression in many tissues suggests that TCTP most likely has a cell housekeeping function.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180127
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