The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Recent developments in the detection of bovine serum albumin
Abstract
Albumin is a globular protein which plays a pivotal role in maintaining plasma pressure and the nutritional balance. Different compounds are transported by binding to albumin in the blood. Also, human health is closely related to the serum albumin concentration in blood plasma or other biological fluids. Due to the high structural similarity with human serum albumin (HSA), bovine serum albumin (BSA) has been widely investigated as a model protein in different fields. Importantly, albumin detection has recently gained huge interest, as this protein serves as an important indicator of cow health, and its milk and meat quality. Also, it is also known as an allergenic and a carrier protein. As a result, it is highly essential to determine bovine albumin in various industries, such as medicine, pharmaceutical, clinical and food. Therefore, the development of new, efficient, fast and straightforward methods for selective detection of BSA is critical. This review seeks to highlight different characteristics of BSA and its importance. Then, by focusing on recent developments made in the last two decades in BSA biosensing and determination methods, the use of different biomaterials/nanomaterials is discussed.
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Static DNA Nanostructures For Cancer Theranostics: Recent Progress In Design And Applications
Jahanban-Esfahlan, R., Seidi, K., Jahanban-Esfahlan, A., Jaymand, M., Alizadeh, E., Majdi, H., Najjar, R., Javaheri, T., & Zare, P. (2019) · Nanotechnology, Science and Applications · doi:10.2147/nsa.s227193 · Cited by 50
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Metadata
- Authors
- Jahanban-Esfahlan, A., Ostadrahimi, A., Jahanban-Esfahlan, R., Roufegarinejad, L., Tabibiazar, M., & Amarowicz, R.
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2019-10
- Volume
- 138
- Pages
- 602-617
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W2957056775
- Cited by
- 304
- References
- 62
- FWCI
- 6.52
- Type
- journal article
- Language
- en
- Open access
- closed
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