By using a graft polymer comprising a dendritic polymer with a styrene skeleton and a hydrophilic polymer grafted to a terminal thereof, a temperature-responsive substrate for cell culture having a temperature-responsive surface for cell culture that allows cells to be cultured with high efficiency and which yet allows cultured cells to be exfoliated in a short period of time and with high efficiency by simply changing the temperature of the substrate surface can be prepared conveniently. If this temperature-responsive substrate for cell culture is used, cells obtained from a variety of tissues can be cultured with high efficiency. If this culture method is utilized, cultured cells can be exfoliated intact in a short amount of time with high efficiency. In addition, by using this graft polymer, a wide range of peptides and proteins can also be separated by simply changing the temperature of a chromatographic carrier. This allows for convenient separation procedure and improves the efficiency of separating operations. What is more, the stereoregularity of the dendritic polymer per se may be utilized to enable separation of solutes based on differences in their molecular structures.

A purification agent which includes a compound having a betaine structure, and which is for a sugar chain having a length equal to or longer than that of a monosaccharide or for a glycopeptide having a sugar chain having a length equal to or longer than that of a monosaccharide.

A method of removing and capturing an acid gas from a fluid stream includes exposing the fluid stream to an aqueous scrubbing solution in the presence of a packing element including alternating hydrophobic and hydrophilic features or zones. A related apparatus is also disclosed.

The present invention relates to the use of redox agents for purification of the CRM 197 variant of diphtheria toxin. The invention further relates to multi-step purification of CRM 197 from bacterial fermentates.

Combinations of different chromatography modalities with particularly refined conditions significantly reduce acid charge variants in a preparation of monoclonal antibodies. The process for reducing acid charge variants utilizes a combination of anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography polishing, whereby the levels of acidic or basic charge species of the monoclonal antibodies may be modulated to a desired level.

Combinations of different chromatography modalities with particularly refined conditions significantly reduce acid charge variants in a preparation of monoclonal antibodies. The process for reducing acid charge variants utilizes a combination of anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography polishing, whereby the levels of acidic or basic charge species of the monoclonal antibodies may be modulated to a desired level.

In certain embodiments, the invention provides a method of purifying a protein of interest from a mixture which comprises the protein of interest and one or more contaminants, said method comprising: a) subjecting the mixture to a first chromatography matrix, wherein the protein of interest binds to the first chromatography matrix; b) contacting the first chromatography matrix with a first wash solution which has a pH of at least 9.0, and does not comprise arginine or an arginine derivative; and c) eluting the protein of interest from the first chromatography matrix into an elution solution.

In certain embodiments, the invention provides a method of purifying a protein of interest from a mixture which comprises the protein of interest and one or more contaminants, said method comprising: a) subjecting the mixture to a first chromatography matrix, wherein the protein of interest binds to the first chromatography matrix; b) contacting the first chromatography matrix with a first wash solution which has a pH of at least 9.0, and does not comprise arginine or an arginine derivative; and c) eluting the protein of interest from the first chromatography matrix into an elution solution.

Solid supports and ligands are provided for purification of biomolecules by mixed-mode anion exchange-hydrophobic chromatography. Compositions can have the formula Support-(X)N(R1, R2)-R3-L-Ar, or a salt thereof, wherein: Support is a chromatographic solid support; X is a spacer or absent; R1 and R2 are each selected from hydrogen and an alkyl comprising 1-6 carbons; R3 is an alkyl comprising 1-6 carbons or a cyclo alkyl comprising 1-6 carbons; L is NR4, O, or S; wherein R4 is hydrogen or an alkyl comprising 1-6 carbons; and Ar is an aryl. Methods are also provided for using solid supports and ligands to purify biomolecules such as monomeric antibodies.

The present invention refers to a method for the separation of peptide aggregates and fragments from solutions containing target peptide.