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  1. Book: In memory of founding editor Prof. George G. "Gerry" Guilbault

    Guilbault, George G

    (Analytical letters : Special issue ; 43.2010,10/11)

    2010  

    Abstract: ... ...

    Series title Analytical letters : Special issue ; 43.2010,10/11
    Abstract Literaturangaben
    Language English
    Size S. 1543 - 1821, Ill., graph. Darst
    Publisher Dekker
    Publishing place New York, NY
    Document type Book
    Note Einzelaufnahme eines Zeitschr.-H.
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  2. Article: Newer Fluorometric Methods for the Analysis of Biologically Important Compounds.

    Guilbault, G G

    Journal of research of the National Bureau of Standards. Section A, Physics and chemistry

    2021  Volume 76A, Issue 6, Page(s) 607–612

    Abstract: Newer fluorometric methods for the analysis of biologically important compounds will be discussed: enzymes such as LDH, alkaline phosphatase, lipase and cholinesterase, and substrates such as glucose, urea and uric acid. These methods are based on the ... ...

    Abstract Newer fluorometric methods for the analysis of biologically important compounds will be discussed: enzymes such as LDH, alkaline phosphatase, lipase and cholinesterase, and substrates such as glucose, urea and uric acid. These methods are based on the production of fluorescence initiated by an enzymic reaction. New reagentless fluorescence methods will be described for enzymes and substrates. These methods are highly precise (1%), fast (less than 1 minute) and involve no preparation of reagents. These methods, as adapted to clinical laboratory procedures, will be discussed.
    Language English
    Publishing date 2021-09-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 241519-7
    ISSN 0022-4332
    ISSN 0022-4332
    DOI 10.6028/jres.076A.053
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

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  3. Article ; Conference proceedings ; Online: USE OF PROTEIN COATINGS ON PIEZOELECTRIC CRYSTALS FOR ASSAY OF GASEOUS POLLUTANTS

    Guilbault, G. / Ngeh-Ngwainbi, J.

    2023  

    Abstract: Preliminary studies utilizing biological substrates, such as enzymes and antibodies, as coatings for a piezoelectric crystal detector have proven successful. Immobilization of cholinesterase and parathion antibodies allows for the detection of ... ...

    Abstract Preliminary studies utilizing biological substrates, such as enzymes and antibodies, as coatings for a piezoelectric crystal detector have proven successful. Immobilization of cholinesterase and parathion antibodies allows for the detection of organophosphorous pesticides at the ppb level with the cholinesterase coatings exhibiting a more specific response to parathion. Excellent reproducibilities, coating lifetimes, response times and selectivities are observed. This research is the first use of proteins as coatings for the direct assay of gaseous compounds, thus making this method an attractive alternative to some conventional techniques currently in use.
    Language English
    Publishing date 2023-08-30
    Publisher GBF - Gesellschaft für Biotechnologische Forschung
    Publishing country de
    Document type Article ; Conference proceedings ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  4. Article: Immobilized enzymes as analytical reagents.

    Guilbault, G G

    Applied biochemistry and biotechnology

    2013  Volume 7, Issue 1-2, Page(s) 85–98

    Abstract: Immobilized enzymes are becoming increasingly popular as analytical reagents because of their reusability, stability, and sensitivity to many inhibitors that would seriously interfere in assays using soluble enzymes. In this article, some of the kinetic ... ...

    Abstract Immobilized enzymes are becoming increasingly popular as analytical reagents because of their reusability, stability, and sensitivity to many inhibitors that would seriously interfere in assays using soluble enzymes. In this article, some of the kinetic and catalytic effects of immobilized enzymes in analysis will be discussed. The shift of the activity-pH profile curves on immobilization, the changes in temperature dependence. the inhibitor constants (K1). Michaelis constants (K m ), and the maximum velocity (Vmax). plus others, will be discussed. Finally, the use of these immobilized enzymes in fluorometric and electrochemical monitoring systems will be shown, and the future of these reagents in various areas will be discussed. A survey of enzyme electrodes will be presented as an example of the use of immobilized enzymes. Application of immobilized enzyme technology to the assay of BUN, glucose, uric acid, amino acids, ethanol. and other metabolites will be discussed.
    Language English
    Publishing date 2013-11-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 392344-7
    ISSN 0273-2289
    ISSN 0273-2289
    DOI 10.1007/BF02798629
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3053: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article: Use of luminescence spectroscopy for assay of pharmaceutical compounds.

    Guilbault, G

    Journal of pharmaceutical and biomedical analysis

    2006  Volume 4, Issue 6, Page(s) 771–775

    Language English
    Publishing date 2006-06-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 604917-5
    ISSN 1873-264X ; 0731-7085
    ISSN (online) 1873-264X
    ISSN 0731-7085
    DOI 10.1016/0731-7085(86)80087-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1850: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Book ; Conference proceedings: Analytical uses of immobilized biological compounds for detection, medical and industrial uses

    Guilbault, George G.

    [proceedings of the NATO Advanced Research Workshop on Analytical Uses of Immobilized Biological Compounds for Detection, Medical and Industrial Uses, Florence, Italy, May 4 - 8, 1987]

    (NATO ASI series : Ser. C ; 226)

    1988  

    Event/congress Advanced Research Workshop on Analytical Uses of Immobilized Biological Compounds for Detection, Medical and Industrial Uses (1987, Florenz)
    Author's details ed. by George G. Guilbault
    Series title NATO ASI series : Ser. C ; 226
    NATO ASI series
    NATO ASI series ; Ser. C
    Collection NATO ASI series
    NATO ASI series ; Ser. C
    Keywords Biochemistry / methods / congresses ; Enzymes, Immobilized / congresses ; Immobilisierung ; Biosensor
    Subject Biochemischer Sensor ; Immobilisation
    Size XV, 396 S. : graph. Darst.
    Publisher Reidel
    Publishing place Dordrecht u.a.
    Publishing country Netherlands
    Document type Book ; Conference proceedings
    HBZ-ID HT003167283
    ISBN 90-277-2660-4 ; 978-90-277-2660-5
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1989 A 699 order for loan Magazin

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  7. Book: Handbook of enzymatic methods of analysis

    Guilbault, George G.

    (Clinical and biochemical analysis ; 4)

    1976  

    Author's details George G. Guilbault
    Series title Clinical and biochemical analysis ; 4
    Collection
    Keywords Enzymatische Analyse
    Language English
    Size XI, 738 S.
    Publisher Dekker
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT004454940
    ISBN 0-8247-6425-0 ; 978-0-8247-6425-8
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1977 A 2210 order for loan Magazin

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  8. Article: Packaging cells for lentiviral vectors generated using the cumate and coumermycin gene induction systems and nanowell single-cell cloning.

    Broussau, Sophie / Lytvyn, Viktoria / Simoneau, Mélanie / Guilbault, Claire / Leclerc, Mélanie / Nazemi-Moghaddam, Nazila / Coulombe, Nathalie / Elahi, Seyyed Mehdy / McComb, Scott / Gilbert, Rénald

    Molecular therapy. Methods & clinical development

    2023  Volume 29, Page(s) 40–57

    Abstract: ... with the vesicular stomatitis virus glycoprotein (VSV-G). A novel gene regulation system, based on the combination of the cumate and ...

    Abstract Lentiviral vectors (LVs) are important for cell therapy because of their capacity to stably modify the genome after integration. This study describes a novel and relatively simple approach to generate packaging cells and producer clones for self-inactivating (SIN) LVs pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G). A novel gene regulation system, based on the combination of the cumate and coumermycin induction systems, was developed to ensure tight control for the expression of cytotoxic packaging elements. To accelerate clone isolation and ensure monoclonality, the packaging genes were transfected simultaneously into human embryonic kidney cells (293SF-3F6) previously engineered with the induction system, and clones were isolated after limiting dilution into nanowell arrays using a robotic cell picking instrument with scanning capability. The method's effectiveness to isolate colonies derived from single cells was demonstrated using mixed populations of cells labeled with two different fluorescent markers. Because the recipient cell line grew in suspension culture, and all the procedures were performed without serum, the resulting clones were readily adaptable to serum-free suspension culture. The best producer clone produced LVs expressing GFP at a titer of 2.3 × 10
    Language English
    Publishing date 2023-02-26
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2872938-9
    ISSN 2329-0501 ; 2329-0501
    ISSN (online) 2329-0501
    ISSN 2329-0501
    DOI 10.1016/j.omtm.2023.02.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 7107: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  9. Article ; Online: Antigenicity of the Mu (B.1.621) and A.2.5 SARS-CoV-2 Spikes.

    Chatterjee, Debashree / Tauzin, Alexandra / Laumaea, Annemarie / Gong, Shang Yu / Bo, Yuxia / Guilbault, Aurélie / Goyette, Guillaume / Bourassa, Catherine / Gendron-Lepage, Gabrielle / Medjahed, Halima / Richard, Jonathan / Moreira, Sandrine / Côté, Marceline / Finzi, Andrés

    Viruses

    2022  Volume 14, Issue 1

    Abstract: The rapid emergence of SARS-CoV-2 variants is fueling the recent waves of the COVID-19 pandemic. Here, we assessed ACE2 binding and antigenicity of Mu (B.1.621) and A.2.5 Spikes. Both these variants carry some mutations shared by other emerging variants. ...

    Abstract The rapid emergence of SARS-CoV-2 variants is fueling the recent waves of the COVID-19 pandemic. Here, we assessed ACE2 binding and antigenicity of Mu (B.1.621) and A.2.5 Spikes. Both these variants carry some mutations shared by other emerging variants. Some of the pivotal mutations such as N501Y and E484K in the receptor-binding domain (RBD) detected in B.1.1.7 (Alpha), B.1.351 (Beta) and P.1 (Gamma) are now present within the Mu variant. Similarly, the L452R mutation of B.1.617.2 (Delta) variant is present in A.2.5. In this study, we observed that these Spike variants bound better to the ACE2 receptor in a temperature-dependent manner. Pseudoviral particles bearing the Spike of Mu were similarly neutralized by plasma from vaccinated individuals than those carrying the Beta (B.1.351) and Delta (B.1.617.2) Spikes. Altogether, our results indicate the importance of measuring critical parameters such as ACE2 interaction, plasma recognition and neutralization ability of each emerging variant.
    MeSH term(s) Angiotensin-Converting Enzyme 2/metabolism ; Antibodies, Neutralizing/immunology ; COVID-19/immunology ; COVID-19/virology ; COVID-19 Vaccines/immunology ; HEK293 Cells ; Humans ; Mutation ; Neutralization Tests ; Protein Binding ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism ; Temperature
    Chemical Substances Antibodies, Neutralizing ; COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2022-01-14
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14010144
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Amperometric determination of urea using an NADH-dependent coupled enzyme.

    Guilbault, G G / Seo, M L

    Talanta

    2006  Volume 41, Issue 6, Page(s) 1029–1033

    Abstract: Enzyme electrodes for the amperometric measurement of urea were prepared by co-immobilizing l-glutamate dehydrogenase and urease onto an Immobilon-AV affinity membrane with attachment to a glassy carbon electrode. Reduced nicotinamide adenine ... ...

    Abstract Enzyme electrodes for the amperometric measurement of urea were prepared by co-immobilizing l-glutamate dehydrogenase and urease onto an Immobilon-AV affinity membrane with attachment to a glassy carbon electrode. Reduced nicotinamide adenine dinucleotide (NADH) was used as the electroactive species. The electrochemical oxidation of NADH was monitored at +1.0 V vs. Ag/AgCl. The enzyme immobilized electrode was linear over the range of 2.0 x 10(-5) to 2 x 10(-4)M. The response time of the electrode was 3 min and the optimum pH of enzyme immobilized membrane was pH 7.4-7.6 (Dulbecco's buffer solution). It was stable for at least two weeks and 50 assays. There were no interferences from other physiological material, except for high levels of ascorbic acid.
    Language English
    Publishing date 2006-01-23
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1500969-5
    ISSN 1873-3573 ; 0039-9140
    ISSN (online) 1873-3573
    ISSN 0039-9140
    DOI 10.1016/0039-9140(94)e0108-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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