An Alternative method of large scale plasma fractionation for the isolation of serum albumin

Schneider, W; Lefèvre, Hans; Fiedler, H.-P.; McCarty, Lee J.

doi:10.1007/bf01633727

Cited by 16 publications

(17 citation statements)

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“…Since the bovine plasma obtained from slaughterhouses shows a high degree of hemolysis, with a dark red color, it is necessary first of all to remove hemoglobin with 0.6% chloroform and 19.0% cold ethanol (-20 o C) at pH 7.2 (8,9). All the globulins (alpha, beta and gamma) are removed by the method of Cohn et al (10) and nonspecific hemagglutinin by thermocoagulation (11). Final purification is performed by liquid chromatography using the anion ion-exchange gel DEAE-Sepharose FF (Pharmacia, Uppsala, Sweden) (8,12,13).…”

Section: Introductionmentioning

confidence: 99%

Isolation of bovine plasma albumin by liquid chromatography and its polymerization for use in immunohematology

Tanaka

Sawatani

Shigueoka

et al. 2001

Braz J Med Biol Res

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The aim of the method described here is to remove hemoglobin, the major contaminant in the bovine plasma obtained from slaughterhouses, by adding a mixture of 19% cold ethanol and 0.6% chloroform, followed by fibrinogen and globulin precipitation by the Cohn method and nonspecific hemagglutinin by thermocoagulation. The experimental volume of bovine plasma was 2,000 ml per batch. Final purification was performed by liquid chromatography using the ionexchange gel DEAE-Sepharose FF. The bovine albumin thus obtained presented ³99% purity, a yield of 25.0 ± 1.2 g/l plasma and >71.5% recovery. N-acetyl-DL-tryptophan (0.04 mmol/g protein) and sodium caprylate (0.04 mmol/g protein) were used as stabilizers and the final concentration of albumin was adjusted to 22.0% (w/v), pH 7.2 to 7.3. Viral inactivation was performed by pasteurization for 10 h at 60 o C. The bovine albumin for the hemagglutination tests used in immunohematology was submitted to chemical treatment with 0.06% (w/v) glutaraldehyde and 0.1% (w/v) formaldehyde at 37 o C for 12 h to obtain polymerization. A change in molecular distribution was observed after this treatment, with average contents of 56.0% monomers, 23.6% dimers, 12.2% trimers and 8.2% polymers. The tests performed demonstrated that this polymerized albumin enhances the agglutination of Rho(D)-positive red cells by anti-Rho(D) serum, permitting and improving visualization of the results.

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Section: Introductionmentioning

confidence: 99%

Isolation of bovine plasma albumin by liquid chromatography and its polymerization for use in immunohematology

Tanaka

Sawatani

Shigueoka

et al. 2001

Braz J Med Biol Res

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“…It is considered to be non-toxic and chemically relatively inert [13]. Schneider and co-workers combined heat fractionation with polyethylene glycol precipitation yielding at least 90% of the original albumin content of the plasma [14].…”

Section: Polyethylene Glycol Precipitationmentioning

confidence: 99%

Medicinal Chemistry Meets Proteomics: Fractionation of the Human Plasma Proteome

Kovács¹,

Guttman²

2013

CMC

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Human plasma and its fractions/derivatives are frequently used materials in biomedicine as it contains thousands and thousands of proteins representing the majority of human proteome. Several important methods were developed in the past for the fractionation of this important biological fluid and their use for medicinal purposes. One of the greatest challenges is the very large dynamic range of plasma proteins ranging up to 10-12 orders of magnitude. Early attempts were mainly based on methods such as salting out or cold ethanol precipitation, as well as chromatography utilizing affinity, size exclusion, ion exchange and hydrophobic interaction techniques. More recently, fractionation applications started with the depletion of the high abundant plasma components, such as serum albumin and immunoglobulins, before isolating lower abundant proteins of interest. Plasma volumes were utilized from the milliliter scale for diagnostic applications to hundreds of liters for industrial scale plasma fractionation (e.g., medicinal product manufacturing). In this paper we review this important part of medicinal chemistry, highlighting the traditional methods along with some of their variations as well as the most significant recent achievements of the field.

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“…These include the use of polyethylene glycol for initial fractionation of plasma fol Ever since Cohn et al [2] followed by Oncley et al [13] developed the cold ethanol procedure for fractionation of plasma into five major fractions, the method for prepar ing clinical albumin from Cohn fraction V has been predominantly used over the past 30 years throughout the world. The albumin thus prepared was carefully characterized by the Protein Foundation and subsequently approved by the Division of Biologies Stand lowed either by electrodecantation [15] or by repeated chromatography on ion ex changers [3], and the method of Schneider et al [16] which involves heating the plas ma in the presence of ethanol and a stabiliz er followed by precipitation of albumin with polyethylene glycol. However, none of these methods has received wide acceptance by the industrial fractionators in the United States.…”

Section: Introductionmentioning

confidence: 99%

A Simple Method for the Preparation of Human Serum Albumin

Hao¹

1979

Vox Sanguinis

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A simple method, based on ethanol fractionation, for the preparation of highly purified human serum albumin with a higher yield than that of the conventional ethanol procedures is described. It consists of two purification steps, namely, precipitation of most of the other plasma proteins from a 3-fold diluted plasma with ethanol at 42% concentration, pH 5.75 and -5°C, leaving over 96% pure albumin in the supernatant, followed by isolectric precipitation of albumin from the supernatant at pH 4.8 and -5°C. The paste thus obtained was processed to the final albumin solution according to the conventional methods. The yield of the final albumin with a purity of over 99% was equivalent to 29.5 g/l of plasma representing a recovery of over 93%. The possibility of recovering other plasma proteins and the suitability for large scale preparation are also discussed.

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An Alternative method of large scale plasma fractionation for the isolation of serum albumin

Cited by 16 publications

References 0 publications

Isolation of bovine plasma albumin by liquid chromatography and its polymerization for use in immunohematology

Isolation of bovine plasma albumin by liquid chromatography and its polymerization for use in immunohematology

Medicinal Chemistry Meets Proteomics: Fractionation of the Human Plasma Proteome

A Simple Method for the Preparation of Human Serum Albumin

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