Large-Scale Production and Properties of Immunoaffinity- Purified Human Activated Protein C Concentrate

Orthner, Carolyn L.; Ralston, Annemarie H.; Gee, Dan M.; Kent, Randy; Kolen, Billy; McGriff, J.D.; Drohan, William N.

doi:10.1159/000462862

Cited by 4 publications

(2 citation statements)

References 30 publications

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“…For preparation of mAb‐immobilized gel, Sepharose Fast Flow (Amersham Pharmacia Biotech) was activated with cyanogen bromide (Nakarai Tesque, Kyoto, Japan) and the mAb was coupled to the activated gel at a mean density of 5 mg of mAb/ml of gel [15]. Anti‐FVII mAb was quantified by sandwich ELISA for murine IgG, using a modification of a previously described procedure [16]. The limit of detection for anti‐FVII mAb was 0·25 ng/ml.…”

Section: Methodsmentioning

confidence: 99%

Large‐scale production and properties of human plasma‐derived activated Factor VII concentrate

et al. 2003

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Section: Methodsmentioning

confidence: 99%

Large‐scale production and properties of human plasma‐derived activated Factor VII concentrate

et al. 2003

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“…Processes to manufacture protein C (PC) from plasma have been developed and PD‐PC concentrates commercialized in Europe for many years for the treatment of patients with deficiency [2,98]. The plasma fractionation industry, however, failed to develop an activated PC (aPC), although thrombin activation of PC could readily be used to prepare stable aPC [99]. Rh‐aPC has been successfully expressed in human embryonic kidney 293 (HEK293) cells.…”

Section: Protease Inhibitors and Anticoagulation Factorsmentioning

confidence: 99%

Recombinant plasma proteins

Burnouf

2010

Vox Sanguinis

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For almost 50 years, the fractionation of human plasma has been the sole possible source of a wide range of therapeutic proteins--such as coagulation factors, anticoagulants, immunoglobulins, and albumin--essential to the treatment of serious congenital or acquired bleeding or immunological diseases. In the last 20 years, the application of recombinant technologies to mammalian cell cultures has made possible--although with some limitations in productivity, costs, and immunogenic risks--to produce and commercialize complex plasma glycoproteins for human therapeutic applications and has opened the way to the development of new molecular entities. Today, the advanced exploration of alternative cell lines and enhanced cell culture systems, as well as the development of alternative expression technologies, such as transgenic animals, is opening a new era in the production of the full range of recombinant plasma protein therapeutics. In this review, we examine the achievements and ongoing challenges of the recombinant DNA technology as a platform for the production of plasma proteins and the advantages and limitations of such products compared to fractionated plasma proteins.

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L-Arginine and L-Glutamic Acid Increase the Content of Protein C in the Early Stages of Isolation From Donor Plasma

Patalakh¹

2021

Biotechnol. acta

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Current large-scale production of blood-derived pharmacological preparations is aimed at expanding the list of products and deeper extraction of target proteins especially at the pre-purification stage. In particular, this problem becomes critical for the isolation of proteins like protein C (PC), which is present in plasma in trace amounts. Aim. We aimed to improve the buffer composition to minimize the interaction of PC with other proteins and lipids that are inevitably present in the stock material. Methods. The content of protein C in plasma and its derivatives was assessed by the amidolytic activity to the chromogenic substrate S2366. A decrease in homologous impurities and plasma enrichment with protein C was provided by selective bulk adsorption on DEAE-cellulose. Results. Here we describe that an equimolar mixture of two amino acids (L-arginine and L-glutamic acid) essentially increased the content of protein C at the stage of cryo-depleted plasma pre-purification, including initial dilution and subsequent enrichment of plasma with protein C due to selective bulk adsorption on DEAE- cellulose. Additionally, it was revealed that solutions of these amino acids, when combined, inhibit the induced amidolytic activity of protein C and increase its solubility (in contrast to other plasma proteases). Conclusion. Pre-adding of a mixture of amino acids L-arginine and L-glutamic acid to cryo-depleted plasma significantly optimizes the pre-purification stage of protein C, providing a 5-fold increase in its yield after elution from DEAE-cellulose.

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Large-Scale Production and Properties of Immunoaffinity- Purified Human Activated Protein C Concentrate

Cited by 4 publications

References 30 publications

Large‐scale production and properties of human plasma‐derived activated Factor VII concentrate

Large‐scale production and properties of human plasma‐derived activated Factor VII concentrate

Recombinant plasma proteins

L-Arginine and L-Glutamic Acid Increase the Content of Protein C in the Early Stages of Isolation From Donor Plasma

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