1975
DOI: 10.1007/bf01633966
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An alternative method of large scale plasma fractionation for the lsolation of serum albumin

Abstract: Human plasma may be separated into five fractions using the method described by Cohn in 1946. Although there are several drawbacks to alcohol precipitation, especially in albumin isolation, it is still used throughout the world. This paper describes an alternative procedure for albumin isolation from plasma or albumin-containing plasma fractions using a combined heat fraction/polyethylene glycol precipitation method. No polyethylene glycol is detected in the final product which is immunoelectrophoretically 100… Show more

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Cited by 41 publications
(3 citation statements)
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“…To date, all protein adsorption studies related to the topic of solution-phase conformational stability have been conducted in fully aqueous conditions, while there is growing attention to the structure and function of proteins in nonaqueous conditions in general, including in areas such as enzymology, pharmaceuticals, and protein purification. , For example, ethanol is a protein precipitant that is widely used in plasma fractionation protocols to yield therapeutic proteins from blood , and can also be used as a solvent to lower the viscosity of antibody formulations . These important applications have spurred interest in understanding how ethanol and other organic solvents affect protein adsorption at solid–liquid interfaces.…”
Section: Introductionmentioning
confidence: 99%
“…To date, all protein adsorption studies related to the topic of solution-phase conformational stability have been conducted in fully aqueous conditions, while there is growing attention to the structure and function of proteins in nonaqueous conditions in general, including in areas such as enzymology, pharmaceuticals, and protein purification. , For example, ethanol is a protein precipitant that is widely used in plasma fractionation protocols to yield therapeutic proteins from blood , and can also be used as a solvent to lower the viscosity of antibody formulations . These important applications have spurred interest in understanding how ethanol and other organic solvents affect protein adsorption at solid–liquid interfaces.…”
Section: Introductionmentioning
confidence: 99%
“…To the first concentrate (through a 30‐kDa cut‐off membrane) was added sodium octanoate (2.3 g per 100 g of protein) and EDTA to a final concentration of 2 mM, the pH was adjusted to 6.5. The temperature of the solution was elevated to 70 °C in 10 min and maintained for 1 h [26–28]. The solution was cooled rapidly in 10 min to 35 °C.…”
Section: Resultsmentioning
confidence: 99%
“…Briefly, cold ethanol fractionation involves reducing the sample temperature to approximately -5 °C followed by the addition of ethanol and adjusting the solution pH and ionic strength in order to isolate BSA protein [27][28][29] . By contrast, heat-shock fractionation involves heating the sample (typically to ~60 °C or slightly higher) in order to isolate BSA protein and is conducted in the presence of a fatty acid stabilizer (caprylic acid) [30][31][32] . These two fractionation processes can be completed alone or sequentially (cold ethanol, then heat-shock).…”
Section: Evaluation Strategymentioning
confidence: 99%