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Optical Nanobiosensors and Nanoprobes
Published in Tuan Vo-Dinh, Nanotechnology in Biology and Medicine, 2017
The production of antibodies requires the use of immunogenic species. For a substance to be immunogenic (i.e., capable of producing an immune response), a certain molecular size and complexity are necessary: proteins with molecular weights >5000 Da are generally immunogenic. Radioimmunoassay (RIA), which utilizes radioactive labels, has been one of the most widely used immunoassay methods. RIA has been applied to a number of fields including pharmacology, clinical chemistry, forensic science, environmental monitoring, molecular epidemiology, and agricultural science. The usefulness of RIA, however, is limited by several shortcomings, including the required use of radioactive labels, the limited shelf life of radioisotopes, the potential deleterious biological effects inherent to radioactive materials, and the cost of radioactive waste disposal. For these reasons, there are extensive research efforts aimed at developing simpler, more practical immunochemical techniques and instrumentation, which offer comparable sensitivity and selectivity to RIA. In the 1980s, advances in spectrochemical instrumentation, laser miniaturization, biotechnology, and fiberoptics research have provided opportunities for novel approaches to the development of sensors for the detection of chemicals and biological materials of environmental and biomedical interest. Since the first development of a remote fiberoptics immunosensor for in situ detection of the chemical carcinogen benzo[a]pyrene (BaP) (1), antibodies have become common bioreceptors used in biosensors today.
Detection Technology
Published in Rick Houghton, William Bennett, Emergency Characterization of Unknown Materials, 2020
Rick Houghton, William Bennett
Radioimmunoassay (RIA) is a highly sensitive laboratory technique used to measure minute amounts of substances. It involves marking an analyte with a radioactive marker and then determining the presence and quantity of the analyte by detection of radioactivity. In this way, an antibody could be coupled to an antigen that contained any one of a number of radioactive atoms. Many medical tests that utilized this principle have been replaced by nonradioactive tests, but the technology can still be applied to detection and quantification of biological material as well as other substances to which an antibody can be attached (Table 3.17).
Glossary of scientific and technical terms in bioengineering and biological engineering
Published in Megh R. Goyal, Scientific and Technical Terms in Bioengineering and Biological Engineering, 2018
Radioimmunoassay (RIA) refers to an assay based on the use of a radioactively labeled antibody, where the amount of radiation detected indicates the amount of target substance present in the sample.
Reproductive outcomes in rat female offspring from male rats co-exposed to rosuvastatin and ascorbic acid during pre-puberty
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Gabriel Adan Araujo Leite, Thamiris Moreira Figueiredo, Tainá Louise Pacheco, Marina Trevizan Guerra, Janete Aparecida Anselmo-Franci, Wilma De Grava Kempinas
Serum was obtained by centrifugation (2000g, 20 min, 4ºC) in a refrigerated device and was frozen at –20ºC until the moment of hormonal measurements. Progesterone, follicle stimulating hormone (FSH) and luteinizing (LH) were determined by double-antibody radioimmunoassay. Plasma LH and FSH concentrations were determined using specific kits provided by the National Hormone and Peptide Program (Harbor-UCLA, USA). The primary antibodies for LH and FSH were anti-rat LH-S10 and FSH-S11 and the references were LH-RP3 and FSH-RP2, respectively. The lower limit of detection (LOD) for LH was 0.04 ng/ml and for FSH, 0.2 ng/ml. The intra-assay coefficients of variation were 3.4% for LH and 3.0% for FSH. Serum concentrations of progesterone were determined using specific kits provided by MP Biomedicals (Orangeburgh, NY, USA). The intra-assay coefficient of variation was 3.6% and the lower LOD 0.02 ng/ml. All samples were measured in the same assay to avoid the inter-assay errors.
Antibody separation using lectin modified poly(HEMA-EDMA) hydrogel membranes
Published in Journal of Biomaterials Science, Polymer Edition, 2018
Esra Feyzioğlu Demir, Cansu Ilke Kuru, Murat Uygun, Deniz Aktaş Uygun, Sinan Akgöl
IgG is a very important molecule, which uses for therapeutic purposes and it takes a part of the huge portion of the human serum. IgG have been applied for the treatment of various disorder such as immunodeficiencies, idiopathic purpura, autoimmune and chronic inflammatory disorders and cancers. IgG have been also preferred as an immunological assay tool such as ELISA, radioimmunoassay, immunosensor and antibody microarrays. All these assays high IgG purity for correct results. Thus, IgG generally separated by using affinity ligands like Protein A and G. However, these ligands are too expensive to practical usage, and their stabilities are very poor. As an alternative, some other ligand systems have been developed and used for the purification studies of IgG. In this study, synthesized p(HEMA-EDMA)-IMEO-Con A HMs had good capability to separate IgG from its aqueous solutions, and were prepared easily from un-expensive precursors by simple methods.
Prostate histological investigation in rats exposed to bisphenol a and phytochemicals during the perinatal period and subjected to hormonal stimulus in adulthood
Published in International Journal of Environmental Health Research, 2022
Thainá Cavalleri Sousa, Camila Bonillo de Oliveira, Maria Luiza Silva Ricardo, Ariana Musa de Aquino, Wellerson Rodrigo Scarano, Allice Santos Cruz Veras, Maria Eduarda Almeida Tavares, Giovana Rampazzo Teixeira, Anthony César deSousa Castillho, Francis Lopes Pacagnelli, Joyce Zalotti Brandt, Leonardo de Oliveira Mendes
After euthanasia on the PDN 300, blood from eight animals from different litters/groups was collected in 15 mL falcon tubes. The material was centrifuged at 3,000 r.p.m., 4°C, for 20 min, and the serum was separated and frozen for further analysis. DHT (Diagnostics Biochem Canada Inc, Canada) serum analysis was performed by enzyme immunoassay (ELISA). At the same time, testosterone was measured by double antibody radioimmunoassay using the Coat-A-Count® kit (Diagnostics Products Corporation, Los Angeles, USA). The intra- and inter-assay variations were 1.75% and 20%, and the analyzes were performed at the Endocrinology Laboratory of the Faculty of Dentistry of Ribeirão Preto/SP – USP.