To provide a means capable of simultaneously and accurately analyzing a component derived from a carrier for liquid phase peptide synthesis with, for example, a target peptide.

A method for simultaneously analyzing a carrier for liquid phase peptide synthesis, a component derived from the carrier for liquid phase peptide synthesis, an amino acid to which the carrier for liquid phase peptide synthesis is bound, and a peptide compound to which the carrier for liquid phase peptide synthesis is bound, with a target peptide or final target peptide, the analysis method using high-performance liquid chromatography or supercritical fluid chromatography using an alcohol as an eluent.

Silica particles have a fine pore size of 1 to 250 Angstrom (?) and comprise a silane group which comprises two groups which are each independently chosen from alkyl, aryl, alkylaryl, heteroalkyl, heteroaryl, and heteroalkylaryl groups. The silica particles are prepared by a method. The silica particles can be used as a stationary phase for purifying a modified conjugated peptide, such as a GLP-1 agonist or a GLP-2 analog.

Silica particles have a fine pore size of 1 to 250 Angstrom (?) and comprise a silane group which comprises two groups which are each independently chosen from alkyl, aryl, alkylaryl, heteroalkyl, heteroaryl, and heteroalkylaryl groups. The silica particles are prepared by a method. The silica particles can be used as a stationary phase for purifying a modified conjugated peptide, such as a GLP-1 agonist or a GLP-2 analog.

An analysis method for mycotoxins including a separation step, a detection step, and an identification step. In the separation step, each component contained in a liquid sample is separated in a column In the detection step, components separated in the separation step are detected by a PDA and a fluorescence detector. In the identification step, total aflatoxin is identified based on a detection signal from the fluorescence detector, and deoxynivalenol is identified based on a detection signal from the PDA.

Methods, kits and devices for separating phospholipids and proteins from small molecules in biochemical samples can feature an apparatus having a wetting barrier, at least one fit and a separation media. For example, an apparatus can include at least one wall defining a chamber having an exit and an entrance; a wetting barrier disposed between the exit and entrance, so as to define a separation media space located between the wetting barrier and the exit and a sample receiving area located between the wetting barrier and the entrance; and a separation media disposed adjacent to the wetting barrier and having a specific affinity for phospholipids. The wetting barrier is adapted to (i) retain the liquid sample and a protein precipitating agent in the sample receiving area under a first force, thereby facilitating the formation of a protein precipitate and a processed sample, and (ii) flow the processed sample through the wetting barrier and separation media under a second force, wherein the second force is greater than the first force, thereby retaining the protein precipitate in the sample receiving area, retaining phospholipids in the separation media, and eluting small molecules.

Methods, kits and devices for separating phospholipids and proteins from small molecules in biochemical samples can feature an apparatus having a wetting barrier, at least one fit and a separation media. For example, an apparatus can include at least one wall defining a chamber having an exit and an entrance; a wetting barrier disposed between the exit and entrance, so as to define a separation media space located between the wetting barrier and the exit and a sample receiving area located between the wetting barrier and the entrance; and a separation media disposed adjacent to the wetting barrier and having a specific affinity for phospholipids. The wetting barrier is adapted to (i) retain the liquid sample and a protein precipitating agent in the sample receiving area under a first force, thereby facilitating the formation of a protein precipitate and a processed sample, and (ii) flow the processed sample through the wetting barrier and separation media under a second force, wherein the second force is greater than the first force, thereby retaining the protein precipitate in the sample receiving area, retaining phospholipids in the separation media, and eluting small molecules.

The present invention provides an analysis method including separating a compound of the formula (1):

##STR00001##

contained in a polyoxyethylene derivative by reversed-phase chromatography, and detecting the compound with an ultraviolet visible spectrometer detector, in which ultraviolet light with a wavelength shorter than 200 nm as the detection wavelength is used, and an acidic substance with a maximum molar absorption coefficient of not more than 20 M.sup.?1cm.sup.?1 at 190 to 200 nm and a pKa of not more than 4 is used as an additive to the mobile phase for analysis.

Adsorptive media for chromatography, particularly ion-exchange chromatography, derived from a shaped fiber. In certain embodiments, the functionalized shaped fiber presents a fibrillated or ridged structure which greatly increases the surface area of the fibers when compared to ordinary fibers. Also disclosed herein is a method to add surface pendant functional groups that provides cation-exchange or anion-exchange functionality to the high surface area fibers. This pendant functionality is useful for the ion-exchange chromatographic purification of biomolecules, such as monoclonal antibodies (mAbs).

Adsorptive media for chromatography, particularly ion-exchange chromatography, derived from a shaped fiber. In certain embodiments, the functionalized shaped fiber presents a fibrillated or ridged structure which greatly increases the surface area of the fibers when compared to ordinary fibers. Also disclosed herein is a method to add surface pendant functional groups that provides cation-exchange or anion-exchange functionality to the high surface area fibers. This pendant functionality is useful for the ion-exchange chromatographic purification of biomolecules, such as monoclonal antibodies (mAbs).

A material for reverse phase chromatography comprises surface modifying apolar and charged groups bound to a solid support, said charged groups being present in amounts of about 0.25 to about 22% of the surface modifying groups, or in amounts of about 0.01 mol/m.sup.2 to 0.8 mol/m.sup.2 referred to the surface of the solid support for a material with a total amount of surface modifying groups of 3.6 mol/m.sup.2. Such material and suitable purification conditions for active pharmaceutical ingredients (APIs) like peptides can be evaluated by (a) determining the isoelectric point (pI) of the API of interest, (b) choosing a pH in a range where the solid phase material is stable, (c) determining the difference pIpH and (d) if the difference pIpH is positive, choosing an anion exchange (AIEX) material, or if the difference pIpH is negative, choosing an cation exchange (CIEX) material.