A functionalized fine fiber is provided. In an embodiment, the functionalized fine fiber is usable in chromatography. The functionalized fine fiber includes a matrix of fine fiber. The fine fibers preferably have an average diameter of less than 2 micron, and each fine fiber preferably has a length of at least 1 millimeter. The fine fibers carry and immobilize functional molecules.

This invention relates to the application of hydroxyapatite chromatography to the purification of at least one antibody from a preparation containing high molecular weight aggregates. Further, this invention relates to an integration of ceramic hydroxyapatite chromatography into a combination chromatographic protocol for the removal of high molecular weight aggregates from an antibody preparation.

This invention relates to the application of hydroxyapatite chromatography to the purification of at least one antibody from a preparation containing high molecular weight aggregates. Further, this invention relates to an integration of ceramic hydroxyapatite chromatography into a combination chromatographic protocol for the removal of high molecular weight aggregates from an antibody preparation.

A novel system for the analysis of molecules and cells, comprising clusters where a non-magnetic particle is supplemented with magnetic particles to form a characteristic pattern, fingerprint or bar code. Methods and devices for formation of such particles are also disclosed.

Disclosed are methods of enriching collagen fragments in a sample comprising combining a sample comprising collagen fragments with a composition comprising any one of the dimeric CHPs described herein, and wherein the first CHP and second CHP bind to and form a triple helix with a collagen fragment; and removing the bound collagen fragments from the dimeric CHP providing a product enriched with collagen fragments. Disclosed are methods of detecting collagen in a sample comprising enriching collagen fragments from a sample, wherein enriching the collagen fragments comprises combining a sample comprising collagen fragments with a composition comprising a dimeric CHP, wherein the dimeric CHP comprises a first CHP and a second CHP, one or more linkers, and a branch point, wherein the collagen fragments bind the dimeric CHP; and detecting the binding of the collagen fragments to the dimeric CHP.

The present invention relates to the use, for affinity purification of an antibody or an fragment of an antibody, of a ligand-substituted matrix comprising a support material and at least one ligand covalently bonded to the support material, the ligand being represented by formula (I)
L-(Sp).sub.v-Ar.sup.1—Am—Ar.sup.2   (I)
wherein L, SP, Ar.sup.1, AM, Ar.sup.2 and v are defined herein.

Provided is a method for control and/or monitoring and/or optimization of a chromatographic process, in which the method comprises at least 2 columns which are operated, alternatingly, wherein this operation can be carried out in that the at least 2 columns are operated in interconnected and disconnected states, wherein the columns switch positions after such a sequence of interconnected and disconnected state, and wherein downstream of at least one, or of each column, a detector is located capable of detecting the desired product and/or impurities when passing the detector.

The present invention provides methods for analyzing a target compound from a biological sample. In one aspect, a method for analyzing a target compound in a biological sample can comprise delivering a biological sample through an affinity column, the affinity column having a binding ligand coupled to a stationary structural support, wherein the affinity column has a high density of the binding ligand per the stationary structural support and wherein the binding ligand has been preselected to cause weak affinity separation zonal retardation of the target compound from the biological sample forming a target compound fraction and a biological sample fraction and detecting the target compound by mass spectrometry.

There is provided a method of identifying a resin for isolating or enriching a protein of interest using affinity chromatography. The method comprises the steps of: i) providing the three-dimensional structure of the protein of interest; ii) determining and/or calculating one or more parameters of the protein of interest in its two- and/or three-dimensional form; iii) determining and/or calculating one or more parameters of one or more resin in their two- and/or three-dimensional form; and iv) selecting a resin expected to bind complementarily to the protein of interest based upon one or more of the parameters of the protein of interest.

The invention relates to a method for separation of biopolymer molecules, particularly biopolymer molecules from the group consisting of mono- a multi-phosphorylated peptides, recombinant peptides/proteins with a polyhistidine tag (His-tag) or with another chemically similar biospecific tag, cysteine-containing peptides/proteins and nucleic acids, in which a biopolymer molecule is bound in a binding solution by a specific binding to a carrier, which contains a core with dimensions in nano- and/or submicro- and/or microscale, which is composed of oxide of at least one transition metal and/or silicon oxide, on whose surface is deposited at least one continuous or non-continuous layer and/or nanoparticles of magnetic metal oxide and/or such nanoparticles are deposited in its inner structure, and subsequently undesirable and non-specifically bound components are washed off at least once from the carrier-bound bio-molecules by a washing solution, whereupon biopolymer molecules are eluted from it by changing pH and/or by using an elution solution. The invention also relates to a carrier for application of this method.