Human Serum Albumin: A Multifunctional Plasma Protein

More, John; Bulmer, M.

doi:10.1002/9781118356807.ch12

Cited by 9 publications

(7 citation statements)

References 100 publications

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“…Its degradation (about 14 g/day) is mainly carried out in muscle tissue, skin, kidney and gastrointestinal tract as well as to a limited extent in the liver. HSA has a pK of 4.8 which means that at physiological pH (~7.4) it ionizes, which explains its high solubility in water [55,56].…”

Section: Human Serum Albuminmentioning

confidence: 99%

“…The remaining thiol group is responsible for about 80% of the antioxidant capacity of albumin, as it is able to neutralize reactive oxygen species (ROS) and nitrogen species (RNS), as well as free radicals. In addition, it has a wide variety of other functions in the body (Figure 1), which explains its designation as a "multifunctional" protein [56]. Typically, HSA shows a higher affinity for low molecular weight, hydrophobic and negatively charged compounds [58,59].…”

Section: Human Serum Albuminmentioning

confidence: 99%

“…HSA generally transports 1 to 2 fatty acids, however, under certain conditions (very intense physical exercise, for example) there may be an increase in transport to 4 or more fatty acids per molecule of HSA. Furthermore, the binding of fatty acids to albumin can cause conformational changes in the plasma protein and may expose the free thiol group that gives it some antioxidant power [56,57]. Fatty acids are not the only endogenous ligands with the ability to bind to HSA [57]; bilirubin, ascorbate, calcium, copper, zinc, chloride, steroid hormones, nitric oxide (NO) are other examples.…”

Section: Human Serum Albuminmentioning

confidence: 99%

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Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

et al. 2021

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The interaction between proteins and drugs or other bioactive compounds has been widely explored over the past years. Several methods for analysis of this phenomenon have been developed and improved. Nowadays, increasing attention is paid to innovative methods, such as high performance affinity liquid chromatography (HPALC) and affinity capillary electrophoresis (ACE), taking into account various advantages. Moreover, the development of separation methods for the analysis and resolution of chiral drugs has been an area of ongoing interest in analytical and medicinal chemistry research. In addition to bioaffinity binding studies, both HPALC and ACE al-low one to perform other type of analyses, namely, displacement studies and enantioseparation of racemic or enantiomeric mixtures. Actually, proteins used as chiral selectors in chromatographic and electrophoretic methods have unique enantioselective properties demonstrating suitability for the enantioseparation of a large variety of chiral drugs or other bioactive compounds. This review is mainly focused in chromatographic and electrophoretic methods using human serum albumin (HSA), the most abundant plasma protein, as chiral selector for binding affinity analysis and enantioresolution of drugs. For both analytical purposes, updated examples are presented to highlight recent applications and current trends.

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Section: Human Serum Albuminmentioning

confidence: 99%

Section: Human Serum Albuminmentioning

confidence: 99%

Section: Human Serum Albuminmentioning

confidence: 99%

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Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

et al. 2021

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“…Many researchers have tried to improve this method by several modifications. [8][9][10][11][12][13] In this research, the rabbits were immunized with BSA. Then the IEC and protein G affinity chromatography were used to isolate and purify the rabbit anti-BSA antibody.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method

Balkani¹,

Shamekhi²,

Raoufinia³

et al. 2016

Adv Pharm Bull

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“…Albumin is obtained from human blood in two main ways: the Cohn fractionation process which exploits the differential solubility of plasma proteins in cold ethanol solutions in which ionic strength and pH are varied, or by column chromatographic methods (reviewed in [ 3 ]). Both of these processes are followed by a pasteurization step where albumin is stabilized by the addition of octanoate and heated to 60°C for 10 hours.…”

Section: Introductionmentioning

confidence: 99%

Octanoate in Human Albumin Preparations Is Detrimental to Mesenchymal Stromal Cell Culture

Wong

MacKenzie

Nelson

et al. 2015

Stem Cells International

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Cell therapies hold great promise as the next major advance in medical treatment. To enable safe, effective ex vivo culture whilst maintaining cell phenotype, growth media constituents must be carefully controlled. We have used a chemically defined mesenchymal stromal cell culture medium to investigate the influence of different preparations of human serum albumin. We examined two aspects of cell culture, growth rate as measured by population doubling time and colony forming ability which is a representative measure of the stemness of the cell population. Albumin preparations showed comparative differences in both of these criteria. Analysis of the albumin bound fatty acids also showed differences depending on the manufacturing procedure used. We demonstrated that octanoate, an additive used to stabilize albumin during pasteurization, slows growth and lowers colony forming ability during ex vivo culture. Further to this we also found the level of Na+/K+ ATPase, a membrane bound cation pump inhibited by octanoate, is increased in cells exposed to this compound. We conclude that the inclusion of human serum albumin in ex vivo growth media requires careful consideration of not only the source of albumin, but also the associated molecular cargo, for optimal cell growth and behavior.

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Human Serum Albumin: A Multifunctional Plasma Protein

Cited by 9 publications

References 100 publications

Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method

Octanoate in Human Albumin Preparations Is Detrimental to Mesenchymal Stromal Cell Culture

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