A Highly Purified Antithrombin III Concentrate Prepared From Human Plasma Fraction IV‐1 by Affinity Chromatography

Lebing, Wytold R.; Hammond, David J.; Wydick, James E.; Baumbach, George A.

doi:10.1111/j.1423-0410.1994.tb01645.x

Cited by 26 publications

(7 citation statements)

References 29 publications

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“…It is a singlechain glycoprotein comprising 432 amino acids, three disulfide bridges and four carbohydrate side chains [1]. The pAT contains 15% of saccharides and its molecular weight is 58 kDa [2,3].…”

Section: Introductionmentioning

confidence: 99%

Recombinant human antithrombin expressed in the milk of non-transgenic goats exhibits high efficiency on rat DIC model

Yang

Han

et al. 2009

J Thromb Thrombolysis

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Plasma-derived antithrombin (pAT) is often used for the treatments of disseminated intravascular coagulation (DIC) patients. In this paper, the recombinant adenovirus vector encoding human antithrombin (AT) cDNA was constructed and directly infused into the mammary gland of two goats. The recombinant human antithrombin (rhAT) was purified by heparin affinity chromatography from the goat milk, and then used in the treatment of thirty lipopolysaccharide (LPS) induced DIC rats. A high expression level of rhAT up to 2.8 g/l was obtained in the milk of goats. After purification, the recovery rate and the purity of the rhAT were up to 54.7 +/- 3.2% and 96.2 +/- 2.7%, respectively. In blood of the DIC rat model treated with rhAT, the levels of antithrombin and thrombin-antithrombin (TAT) were augmented significantly; meanwhile the consumption of fibrinogen and platelet was reduced significantly, and the increase of alanine aminotransferase (ALT) and aspartate aminotransferase (AST) concentration was restrained modest and non-significant. For the above DIC indexes, there were no differences between pAT and rhAT (P > 0.05). Our results demonstrated that the way we established is a pragmatic tool for large-scale production of rhAT, and the rhAT produced with this method has potential as a substitute for pAT in the therapy of DIC patients.

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Section: Introductionmentioning

confidence: 99%

Recombinant human antithrombin expressed in the milk of non-transgenic goats exhibits high efficiency on rat DIC model

Yang

Han

et al. 2009

J Thromb Thrombolysis

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“…Other examples of chromatographically purified licensed plasma proteins include alpha 1‐antitrypsin ( α 1‐AT) , C1‐esterase inhibitor and factor XI , and other proteins of potential therapeutic interest, but not licensed, such as the inter alpha trypsin inhibitor . In most situations, but not always these proteins are extracted from cryo‐poor plasma rather than from fractions, such as fraction IV‐1, subjected to ethanol precipitation steps as conditions used may alter protein's function or conformation. Reviews on the use of chromatography in plasma fractionation are available for further details .…”

Section: Fractionation Technologiesmentioning

confidence: 99%

mentioning

confidence: 99%

Current status and new developments in the production of plasma derivatives

Burnouf

2016

ISBT Science Series

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Plasma fractionation is a unique biotechnology and bioengineering industry characterized by its capacity to extract a diverse range of protein therapeutics that are often the only options for treating life‐threatening pathological conditions of patients suffering from bleeding, immunological disorders, infections or trauma. Current plasma products include several coagulation factors, polyvalent and hyperimmune immunoglobulins (Igs), albumin, protease inhibitors and anticoagulants. In many pathological situations, these products are used for long‐term replacement therapy to compensate for a congenital or acquired protein deficiency. Most products are obtained by plasma fractionation technologies that derive from the cold ethanol fractionation process developed in the mid‐/late 1940s by Cohn and collaborators. Still, in the last 20 years, this core technology has undergone substantial evolutions illustrated by the integration of several viral reduction steps for all products and by the introduction of chromatographic purification steps to extract labile proteins from cryoprecipitate‐poor plasma. The most recent technological changes, intended mostly to improve recoveries and remove trace protein contaminants, concern the production process of intravenous Igs through implementing chromatographic steps and caprylic acid treatment in early stages of the ethanol fractionation process. A number of new fractionation technologies are currently under development and have not been licensed at least for the time being by major regulatory authorities. One target of these technologies is to improve the recovery of the most important plasma protein products, under conditions facilitating large‐scale implementation in emerging countries.

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“…As a working hypothesis, we therefore assumed that the salt tolerance and higher affinity for plasma proteins are interrelated and dependent on the presence of this sulfate group. [ 17–22 ]…”

Section: Introductionmentioning

confidence: 99%

Salt‐tolerant cation exchanger‐containing sulfate groups as a viable alternative for mixed‐mode type and heparin‐based affinity resins

Begić

Pečenković

Gajdošik

et al. 2021

Biotechnology Journal

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Ion‐exchange chromatography is still one of the most popular protein separation techniques. Before chromatographic separation, the high salt concentration in various samples necessitates additional steps. Therefore, low salt tolerance of ion‐exchange resins is a drawback that needs to be addressed. Herein, the differences in salt tolerance and hydrophobicity of strong cation‐exchange TOYOPEARL resins of sulfonium and sulfate‐types were investigated. Despite only a minor structural difference, differences in selectivity and salt tolerance between the sulfate and sulfonic groups were detected. In silico calculations were also carried out for model substances representing the sulfonium and sulfate groups, wherein significant differences in hydrophobicity was observed. These experiments confirmed the hypothesis that the salt tolerance, higher affinity, and selectivity for certain vitamin K dependent clotting factors are interrelated and dependent on the presence of the sulfate group. Separation of clotting factor IX from the prothrombin complex concentrate further to confirmed the affinity for these proteins. The results show that the use of only a resin with the sulfate ligand and not with the sulfonic acid ligand allows for a facile and rapid separation of clotting factor IX and other vitamin K dependent clotting factors.

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A Highly Purified Antithrombin III Concentrate Prepared From Human Plasma Fraction IV‐1 by Affinity Chromatography

Cited by 26 publications

References 29 publications

Recombinant human antithrombin expressed in the milk of non-transgenic goats exhibits high efficiency on rat DIC model

Recombinant human antithrombin expressed in the milk of non-transgenic goats exhibits high efficiency on rat DIC model

Current status and new developments in the production of plasma derivatives

Salt‐tolerant cation exchanger‐containing sulfate groups as a viable alternative for mixed‐mode type and heparin‐based affinity resins

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