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  • Two-dimensional polyacrylamide gel electrophoresis  (10)
  • Inorganic Chemistry  (5)
  • 1
    Electronic Resource
    Electronic Resource
    cis- und trans-3-Dimethylamino-cyclobutanol-(1) (1962)
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 95 (1962), S. 2535-2540 
    Details
    ISSN: 0009-2940
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: cis- und trans-3-Dimethylamino-cyclobutanol-(1) wurden hergestellt und ihre Diphenylessigsäureester auf spasmolytische Aktivität geprüft.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cber.19620951028
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  • 2
    Electronic Resource
    Electronic Resource
    A Synthetic and Theoretical Study of the Aggregation of Amidoaluminium Hydrides: Solid-State Structure of the Trimethylamine Adduct [(Me3Si)2NA1(Cl)(H) · NMe3] (1996)
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 129 (1996), S. 545-549 
    Details
    ISSN: 0009-2940
    Keywords: Alane ; Association ; Hydride ; Amido ; Amide ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The amidoaluminium hydride complexes [(Me3Si)2NA1(X)(H) · NMe3], X = H (1), Cl (2), were prepared by the metallation of bis(trimethylsilyl)amine by Al(X)(H)2 · NMe3 (X = H and Cl). The molecular structure of 2 as a monomeric Lewis base adduct with four-coordinate aluminium centres and terminal amido groups was confirmed by X-ray crystal structure determination. We also find that bis(trimethylsilyl)amine forms a thermally stable adduct of alane, (Me3Si)2N(H) · AlH3 (3). Ab initio molecular orbital calculations on the possible products arising from these reactions yielding 1 and 2 revealed that the amido-bridged species, {(μ-H2N)Al(X)H}2 (X = H and Cl), are favoured over nitrogen donor Lewis base adduct formation, H2NAl(X)(H) · NH3 (X = H and Cl), and then chloro-bridged, {H2NAl(μ-X)(H)}2, (X = Cl only), and hydrido-bridged species, {H2NAl(X)(μ-H)}2 (X = H and Cl).
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cber.19961290511
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  • 3
    Electronic Resource
    Electronic Resource
    Sequence analysis of wheat grain allergens separated by two-dimensional electrophoresis with immobilized pH gradients (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1115-1119 
    Details
    ISSN: 0173-0835
    Keywords: Bakers' asthma ; Wheat grain allergens ; Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradients ; Protein sequencing ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Micropreparative two-dimensional (2-D) gel electrophoresis with immobilized pH gradients (4-8) in the first dimension (IPG-DALT) was optimized for the separation of salt-soluble wheat grain proteins associated with bakers' asthma disease. The resolved polypeptides were electroblotted onto a polyvinylidene difluoride (PVDF) membrane and incubated with the pooled sera from four asthmatic bakers. Bound IgE was demonstrated by alkaline phosphatase conjugated anti-human IgE. Major IgE binding was detected in the 27 kDa, 37 kDa and, to a lesser extent, in the 14-18 kDa area of the 2-D immunoblots, respectively. Since the main purpose of our study was to determine the N-terminal amino acid sequences of the major wheat grain allergens, N-terminal sequencing was performed for six out of a total of eleven major allergens located in the 27 kDa area, for one out of two 37 kDa allergens, and for two out of four 14-18 kDa allergens. Our results revealed that two of the 27 kDa polypeptides are clearly related to several Acyl-CoA oxidase variants of barley and rice, whereas no significant homologies were found for the remaining four 27 kDa allergens analyzed. The N-terminus of the 37 kDa allergen appeared to be blocked so that no sequence information was obtained, while the two 14-18 kDa allergens analyzed were identified as members of the wheat α-amylase-inhibitor family.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601188
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  • 4
    Electronic Resource
    Electronic Resource
    Coelectrophoresis of cardiac tissue from human, dog, rat and mouse: Towards the establishment of an integrated two-dimensional protein database (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1524-1529 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Heart ; Comigration ; Protein database ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: We have investigated the feasibility of identifying homologous proteins in whole tissue protein extracts of dog, mouse and rat hearts by comparison with our human heart two-dimensional (2-D) database. Samples of ventricular myocardial tissue from each of these species were coelectrophoresed with a human tissue sample. Gels were silver stained and patterns were analysed using PDQUEST. The number of proteins comigrating with human proteins was 301, 201 and 356 for the dog, mouse and rat, respectively. In the dog pattern, 33 of these comigrating proteins were tentatively identified from the similarity between their migration properties and those of known human proteins. Twentynine such proteins were identified in the mouse pattern while 30 comigrating rat proteins were identified. While these tentative identifications require confirmation, we feel that this technique offers a useful shortcut in the characterisation of proteins present in similar tissue samples from different species and avoids the necessity for duplicating laborious procedures, such as protein microsequencing, otherwise used in the identification of these proteins in each species.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601252
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  • 5
    Electronic Resource
    Electronic Resource
    Darstellung und Eigenschaften der Aluminium-Oxid- und -Thiohalogenide Erzeugung eines Oxid- und eines Thioamids (1963)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 323 (1963), S. 1-12 
    Details
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: The aluminium oxyhalides and thiohalides AlOCl, AlOBr, AlOJ, AlSCl, AlSBr, and AlSJ have been prepared and investigated.The reaction with NH3 yields an oxyamid and thioamide, with H2NCH3 a methyl oxyamid and methyl thioamide, respectively.
    Notes: Drei Aluminiumoxidhalogenide - AlOCl, AlOBr und AlOJ - werden dargestellt und eingehend untersucht. In ähnlicher Weise werden die Thiohalogenide - AlSCl, AlSBr und AISJ - bearbeitet. Einwirkung von NH3 führt zu einem Oxidamid bzw. Thioamid, von NH2(CH3) zu einem Methyloxidamid bzw. Methylthioamid.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19633230102
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  • 6
    Electronic Resource
    Electronic Resource
    HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog heart proteins (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2795-2802 
    Details
    ISSN: 0173-0835
    Keywords: Databases ; Dog ; Heart proteins ; Two-dimensional polyacrylamide gel electrophoresis ; World Wide Web ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A two-dimensional gel electrophoresis database of dog (Canis familiaris) proteins is presented. The database contains 1212 protein spots which have been characterised in terms of their pI and Mr. This database has been integrated into the HSC-2DPAGE database which is accessible on the Internet via the World Wide Web with the uniform resource location (URL): (http://www.harefield.nthames.nhs.uk/nhli/protein/index.html). Identifications for 80 of the protein spots have been obtained by visual cross-matching with the human heart protein database in HSC-2DPAGE (42 spots), N-terminal microsequence analysis (25 spots) and peptide mass fingerprinting (20 spots). This database is being used in studies of alterations in protein expression in models of heart failure and heart disease.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181514
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  • 7
    Electronic Resource
    Electronic Resource
    Latex allergen database (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2803-2810 
    Details
    ISSN: 0173-0835
    Keywords: Latex allergy ; Two-dimensional polyacrylamide gel electrophoresis ; Immunoblotting ; Protein microsequencing ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional (2-D) electrophoresis followed by immunoblotting and N-terminal protein microsequencing were used to characterize and identify the IgE-reactive proteins of Hevea latex that are the main cause of the latex type I allergy affecting especially health care workers and spina bifida children. This approach generated a comprehensive latex allergen database, which facilitated the integration of most of the latex allergen data presented in the literature. The major latex allergens Hev b 1, Hev b 3, Hev b 6 and Hev b 7 have been localized on our 2-D maps. Moreover, we were able to identify six previously undescribed IgE-binding latex proteins, namely enolase, superoxide dismutase, proteasome subunit C5, malate dehydrogenase, triosephosphate isomerase and endochitinase. The generated latex 2-D maps will provide valuable information to develop strategies for the isolation of the novel IgE binding proteins in order to study the frequency of sensitization among both risk groups. Detailed knowledge of all proteins involved in latex allergy will allow better diagnosis of latex allergy and to monitor the success of prevention strategies that are needed to reduce the high prevalence of latex allergy among both risk groups.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181515
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  • 8
    Electronic Resource
    Electronic Resource
    The analysis of myocardial proteins by infrared and ultraviolet laser desorption mass spectrometry (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 424-431 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Myocardial proteins ; Infrared laser ; Matrix-assisted laser desorption mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The use of infrared (IR) and ultraviolet (UV) matrix-assisted laser desorption (MALDI) mass spectrometry to analyse myocardial proteins separated by two-dimensional (2-D) polyacrylamide gel electrophoresis (PAGE) is discussed. Proteins were electroblotted onto a FluoroTrans polyvinylidene difluoride (PVDF) membrane in order to facilitate analysis by MALDI, which represented the most efficient means of extracting large numbers of proteins simultaneously. Once on a FluoroTrans membrane, IR-MALDI was used to obtain spectra from selected protein spots, but no useful signals were obtained with UV MALDI. Spectra were generated from 46 of 50 spots analysed with protein masses from 13 to 82 kDa and isoelectric points (pI) 4.7-7.8. For those protein spots that had previously been characterised, and for which both sequence and post-translational modification data were known, IR-MALDI data was within plus or minus 0.5% of the expected mass. Some spots contained more than one protein signal, illustrating the increased information obtainable from MALDI, but also suggesting the limit of resolution of 2-D gels for separating large numbers of proteins. Attempts to digest proteins with specific proteases and generate peptide mass fingerprints by MALDI analysis on the membrane were unsuccessful with either IR or UV lasers. The peptides were extracted from the membrane and readily analysed by UV MALDI for peptide spectra. Poor data was obtained for peptide digests with IR-MALDI, probably because of matrix suppression by digest buffer. In order to obtain the maximum amount of information from blotted proteins, both IR and UV MALDI were required.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180317
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  • 9
    Electronic Resource
    Electronic Resource
    Construction of HSC-2DPAGE: A two-dimensional gel electrophoresis database of heart proteins (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 471-479 
    Details
    ISSN: 0173-0835
    Keywords: Endothelial proteins ; Heart proteins ; Myocyte proteins ; Two-dimensional electrophoresis protein databases ; Two-dimensional polyacrylamide gel electrophoresis ; World Wide Web ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The dissemination of information relating to the characterisation of proteins from two-dimensional electrophoresis (2-DE) gel databases is essential for their effective utilisation in the study of protein expression in cell biology. Since the inception of the World Wide Web and the pioneering development of SWISS-2DPAGE as a tool for retrieving information on proteins separated by 2-DE, the Internet has become the method of choice for disseminating and accessing information on 2-DE protein databases. At Harefield we have established HSC-2DPAGE which is an advanced interface for accessing protein databases relating to heart disease. The Web site currently includes databases of proteins from human, dog and rat ventricular tissue and a human endothelial cell line. The databases are searchable individually or as a whole by remote keyword searches. Each database is represented by both synthetic (computer generated) and real (scanned gel) clickable images upon which characterised protein spots are highlighted by hyperlinked symbols. The database conforms to all the rules proposed for federated 2-DE protein databases and individual protein entries are linked to other protein databases such as SWISS-PROT by active cross-references. This paper describes the construction of HSC-2DPAGE, its maintenance, and access via the Internet.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180322
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  • 10
    Electronic Resource
    Electronic Resource
    Cardiac protein abnormalities in dilated cardiomyopathy detected by two-dimensional polyacrylamide gel electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2031-2042 
    Details
    ISSN: 0173-0835
    Keywords: Dilated cardiomyopathy ; Human heart ; Ischaemic heart disease ; Protein expression ; Two-dimensional polyacrylamide gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The aim of the investigation was to determine whether there are specific global quantitative and qualitative changes in protein expression in heart tissue from patients with dilated cardiomyopathy (DCM) compared with ischaemic heart disease and undiseased tissue. Two-dimensional (2-D) polyacrylamide gel electrophoresis and computer analysis was used to study protein alteration in DCM biopsy material (n=28) compared with donor heart biopsy samples (n=9) and explanted hearts from individuals suffering from ischaemic heart disease (IHD; n = 21). A total of 88 proteins displayed decreased abundance in DCM versus IHD material while five proteins had elevated levels in the DCM group (p〈0.01). The most prominent changes occurred in the contractile protein myosin light chain 2 and in a group of proteins identified as desmin. These changes do not appear to be artefactual degradation events occurring during sample processing. These proteins are not apparent in electrophoretic separations of vascular tissue or cultured endothelial cells, mesothelial cells or cardiac fibroblasts, which are clearly distinguishable from the 2-D protein patterns of whole heart and of isolated cardiac myocytes and do not appear to reflect variations in the cellular composition of biopsy samples. The different protein patterns observed in cardiomyopathy showed no obvious relationship with New York Heart Association (NYHA) functional class or haemodynamic parameters. The study has demonstrated significant alterations in quantitative protein expression in the DCM heart which would have serious implications for myocyte function. These changes might be explained by altered protease activity in DCM which could exacerbate contractile dysfunction in the failing heart.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191123
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