The present invention provides a method for the production of whey proteins in a single step process using combination of chromatography and membrane filtration technique, comprising treating cotton cloth with a mixture of chlorosulphonic acid and chloroform and then subsequently treating it with chloroform, dilute NaOH, glycine and water to recover modified cotton cloth as the product, thereafter fixing product in a membrane filtration device equipped with modified flow pattern and then equilibrating it with equilibration buffer, followed by loading of whey for adsorption of protein on the product and washing of the product with equilibration buffer, thereafter elution of adsorbed proteins with elution buffer, and then regeneration of the product by treating it with dilute HCl and water to reuse the product.

A polyalkylene glycol derivative with a minimal impurity content is prepared simply by the steps of reacting a compound having formula (III-I) or (III-II) with an electrophile having formula (IV) in the presence of an optional basic compound, to form a reaction solution containing a compound having formula (V), and passing the reaction solution through a column of cation and anion exchange resins to remove water-soluble impurities, for thereby purifying the desired polyalkylene glycol derivative.
R.sup.1R.sup.2OR.sup.3O.sub.n-1R.sup.3O.sup.M.sup.+(III-I)
R.sup.1R.sup.2OR.sup.3O.sub.n-1R.sup.3OH(III-II)
R.sup.4R.sup.5X(IV)
R.sup.1R.sup.2OR.sup.3O.sub.nR.sup.5R.sup.4(V)

A polyalkylene glycol derivative with a minimal impurity content is prepared simply by the steps of reacting a compound having formula (III-I) or (III-II) with an electrophile having formula (IV) in the presence of an optional basic compound, to form a reaction solution containing a compound having formula (V), and passing the reaction solution through a column of cation and anion exchange resins to remove water-soluble impurities, for thereby purifying the desired polyalkylene glycol derivative.
R.sup.1R.sup.2OR.sup.3O.sub.n-1R.sup.3O.sup.M.sup.+(III-I)
R.sup.1R.sup.2OR.sup.3O.sub.n-1R.sup.3OH(III-II)
R.sup.4R.sup.5X(IV)
R.sup.1R.sup.2OR.sup.3O.sub.nR.sup.5R.sup.4(V)

Open tubular capillary columns for liquid and ion chromatography, based upon an ionically impermeable polyolefin capillary having a bore with a sulfonate-group- or amine-group-functionalized internal surface. The capillary columns may include a coating of ion exchanging nanoparticles electrostatically bound to the functionalized internal surface. The capillary columns may be made by exposing the interior surface to a sulfonating reagent comprising chlorosulfonic acid (ClSO.sub.3H), preferably from 85 wt % to 95 wt % chlorosulfonic acid at a process temperature of 20 to 25 C. The interior surface may be subsequently exposed to an asymmetrical diamine to form a sulfonic mid-linkage to the diamine, i.e., to form a sulfonamide-linked, amine-group-functionalized internal surface. The coating may be provided by subsequently exposing the interior surface to an aqueous suspension of ion exchanging nanoparticles to electrostatically bond the ion exchanging nanoparticles to the functionalized internal surface.

Open tubular capillary columns for liquid and ion chromatography, based upon an ionically impermeable polyolefin capillary having a bore with a sulfonate-group- or amine-group-functionalized internal surface. The capillary columns may include a coating of ion exchanging nanoparticles electrostatically bound to the functionalized internal surface. The capillary columns may be made by exposing the interior surface to a sulfonating reagent comprising chlorosulfonic acid (ClSO.sub.3H), preferably from 85 wt % to 95 wt % chlorosulfonic acid at a process temperature of 20 to 25 C. The interior surface may be subsequently exposed to an asymmetrical diamine to form a sulfonic mid-linkage to the diamine, i.e., to form a sulfonamide-linked, amine-group-functionalized internal surface. The coating may be provided by subsequently exposing the interior surface to an aqueous suspension of ion exchanging nanoparticles to electrostatically bond the ion exchanging nanoparticles to the functionalized internal surface.

Provided is a resin composition comprising (a) a collection of resin beads, wherein the collection of resin beads has pH of 8 or above, and wherein the collection of resin beads has volume average diameter of 150 m to 2,000 m; and (b) a collection of inorganic particles, wherein the inorganic particles contain one or more alkaline earths, and wherein the collection of inorganic particles has volume average diameter of 0.5 m to 50 m.

Also provided is a method of processing an aqueous composition using such a composition.

Proteins are purified by a mixed-mode chromatography system formed by attaching a ligand comprising benzamidoacetic acid to a large-pore support matrix, the only linkage between the ligand and the support matrix being a chain having a backbone of no more than three atoms between a phenyl ring and the support matrix.

Proteins are purified by a mixed-mode chromatography system formed by attaching a ligand comprising benzamidoacetic acid to a large-pore support matrix, the only linkage between the ligand and the support matrix being a chain having a backbone of no more than three atoms between a phenyl ring and the support matrix.

Methods for purifying multispecific antibodies on interest (MAIs) that co-engage at least two different antigens or epitopes (also referred to targets, used interchangeably throughout), from compositions comprising the MAI and parental homodimeric antibody species are provided, as well as reagents which may be used to practice such methods.

Methods for purifying multispecific antibodies on interest (MAIs) that co-engage at least two different antigens or epitopes (also referred to targets, used interchangeably throughout), from compositions comprising the MAI and parental homodimeric antibody species are provided, as well as reagents which may be used to practice such methods.