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![Quantification of Active Antibody Immobilized on Gold Nanoparticles için kapak resmi Quantification of Active Antibody Immobilized on Gold Nanoparticles için kapak resmi](/client/assets/d79c3e4af2b6d196/ctx/images/no_image.png)
Quantification of Active Antibody Immobilized on Gold Nanoparticles
Başlık:
Quantification of Active Antibody Immobilized on Gold Nanoparticles
Yazar:
Tripathi, Kiran, author.
ISBN:
9780438109506
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (93 pages)
Genel Not:
Source: Masters Abstracts International, Volume: 57-06M(E).
Advisors: Jeremy D. Driskell Committee members: Jon Friesen; Christopher Mulligan.
Özet:
Immunoassays are essential tools for basic research in life sciences and in clinical diagnostics. This method has been widely used in several key areas such as diagnosis of diseases, therapeutic drug monitoring and clinical tests. Gold nanoparticle (AuNP) enabled immunoassays have the potential to offer rapid results that can be employed in the field. AuNP-based immunoassays generate highly sensitive results due to the unique optical and electronic properties of nanoparticles. The conjugation of nanoparticles with antibodies (Abs) combines the properties of the nanoparticles themselves with the specific and selective recognition ability of the antibodies to antigens. The activity and stability of the antibody adsorbed onto the gold nanoparticle is important for the functionality of the immunoassay. There are several methods available in the literature for the quantification of immobilized antibodies such as surface plasmon resonance, fluorescence labeling, and the modified Bradford assay, but few methods exist to evaluate their activity.
The focus of this work was to develop a simple and sensitive method to quantify the number of antibodies conjugated to gold nanoparticles (AuNPs) and the fraction of antibodies that maintain antigen-binding activity after immobilization. To this end, anti-HRP antibodies were added to AuNPs to allow for conjugation. The AuNP conjugates were centrifuged, and the supernatant was analysed to indirectly quantify the number of Abs immobilized on the AuNP. To determine the number of binding sites on conjugated Ab, excess horseradish peroxidase (HRP) was added to the conjugate to saturate all available Ab binding sites. After removing excess unbound HRP, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), a substrate for the HRP enzyme, was added to the conjugates. The rate of the enzymatic reaction was determined from absorption of products and directly correlated with the number of HRP captured. The developed method was used to investigate the effects of AuNPs size, Ab types, pH and immobilization methods on the activity of immobilized antibody.
Notlar:
School code: 0092
Konu Başlığı:
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(689765.1) | 689765-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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