Abstract:
An assembly capable of capturing and purifying expressed biological products during or at the end of a bioreaction cycle is disclosed wherein a binding resin is kept separated from the contents of the bioreactor allowing capturing, harvesting and purification of biological products in a bioreactor; the invention additionally provides means of removing undesirable metabolic products as well as provides for efficient loading of chromatography columns.
Abstract:
Methods of inactivation of a virus in a sample comprising a protein component are provided. Also provided are methods of reducing protein degradation or modification in to the presence of a reactive species, such as a reactive species generated as a result of UV exposure, are also provided. In another aspect, a method of reducing oxidation of methionine residues, tryptophan residues or both methionine and tryptophan residues in a protein subjected to UV light is provided. The disclosed methods can be performed at any scale and can be automated as desired.
Abstract:
The present invention provides a process for purifying FV starting from human plasma or a fractionation intermediate thereof, that is simple, scalable to the industrial level and relatively inexpensive compared to the methods described in the literature to date. The invention consists of the use of two anion exchange chromatography steps, the first of which has the purpose of separating the FV from the PTC component factors, while the second has the purpose of isolating the protein of interest from the majority of plasma proteins by means of selective interaction with the weak anion exchange support used. The process developed has also had a viral inactivation step and a viral removal step included, contributing to the safety of the final product obtained, without however significantly altering the process total recovery of FV, and without necessitating the introduction of additional steps for eliminating the inactivating agents used, thanks to the order in which the various steps are conducted. The process described in the present invention also enables an FV concentrate to be obtained that is stable once frozen at -20° C.
Abstract:
The invention concerns a bag comprising a first conduit (13J), a second conduit (13K), the first section ( 13 J 1 ) of the first conduit (13J) and the first section (13K1 ) of the second conduit (13K) being opposite; a third conduit (13L) linking said first respective ends (13J2, 13K2) of said first respective sections (13J1, 13K1 ); a fourth conduit (13M) linking said second respective ends (13J3, 13K3) of said first respective sections (13J1, 13K1 ); a fifth conduit (13N) linking both said second end (13J3) of said first section ( 13 J 1 ) and said first end (13M1 ) of said fourth conduit (13M), and said fifth conduit (13N) linking both said first end (13K2) and said second end (13L2) of said third conduit (13L); said first conduit (13J) and said second conduit (13K) each being connected to a chromatography column connector (1 1 M).
Abstract:
The present invention relates to a method for isolating and/or purifying at least one polypeptide from a sample comprising polypeptides, characterized in that the sample is brought in contact with a boron carbide carrier material at a ph-value allowing the binding of the polypeptide to the boron carbide carrier material. An associated isolation can be used for example to remove polypeptides from a sample or for purifying polypeptides and/or for concentrating them. The invention further relates to a matrix comprising a boron carbide carrier material for purifying polypeptides.
Abstract:
A method for the purification of a protein, in particular an IgM antibody, which comprises a chromatography step using a non-ionic polymer (such as hydroxyapatite chromatography and polyethylene glycol as the polymer) to remove protein aggregates, followed by an ion exchange chromatography step using a solubility enhancing additive such as a urea compound, an alkylene glycol or a zwitterion, especially glycine.
Abstract:
Beschrieben wird die Verwendung eines Schichtdoppelhydroxids ausgewählt aus der Gruppe bestehend aus natürlichen und synthetischen Hydrotalciten und Verbindungen mit einer Hydrotalcit ähnlichen Struktur, wobei das Schichtdoppelhydroxid in uncalcinierter Form und in Carbonatform vorliegt, und wobei das Mol-Verhältnis von Mg 2+ zu Al 3+ im Schichtdoppelhdydroxid bei maximal 2,5:1 liegt, zur An- oder Einlagerung einer Verbindung ausgewählt aus der Gruppe bestehend aus Biomolekülen, insbesondere Peptiden, Depsipeptiden, Peptidnukleinsäuren (PNAs) und Proteinen.